Variant CBH I polypeptides

ABSTRACT

In alternative embodiments, the invention provides polypeptides having a lignocellulolytic (lignocellulosic) activity, e.g., a ligninolytic and cellulolytic activity, including, e.g., a glycosyl hydrolase, a cellulase, an endoglucanase, a cellobiohydrolase (cbhl) (e.g., an exo-cellobiohydrolase, e.g., having an “exo” activity that can processively release cellobiose units β-1,4 glucose-glucose disaccharide), a beta-glucosidase, a xylanase, a mannanse, a xylosidase (e.g., a (β-xylosidase) and/or an arabinofuranosidase activity, polynucleotides encoding these polypeptides, and methods of making and using these polynucleotides and polypeptides. In one embodiment, the invention provides thermostable and thermotolerant forms of polypeptides of the invention. The polypeptides and nucleic acids of the invention are used in a variety of pharmaceutical, agricultural and industrial contexts; for example, as enzymes for the bioconversion of a biomass, e.g., lignocellulosic residues, into fermentable sugars, where in one aspect these sugars are used as a chemical feedstock for the production of ethanol and fuels, e.g., biofuels, e.g., synthetic liquid or gas fuels, including ethanol, methanol and the like.

1. CROSS REFERENCE TO RELATED APPLICATIONS

The present application claims the benefit of national stage applicationfiled in compliance with 35 U.S.C. §371 of International Application No.PCT/US2011/055180, filed Oct. 6, 2011, which claims benefit under 35U.S.C. §119(3) of U.S. Provisional Application No. 61/390,392, filedOct. 6, 2010, and are herein incorporated in their entireties for allpurposes.

2. FIELD OF THE INVENTION

This invention relates to molecular and cellular biology andbiochemistry. In alternative embodiments, the invention providespolypeptides having a lignocellulolytic (lignocellulosic) activity,e.g., a ligninolytic and cellulolytic activity, including, e.g., acellulase or a cellobiohydrolase (cbhl) (e.g., an exo-cellobiohydrolase,e.g., having an “exo” activity that can processively release cellobioseunits β-1,4 glucose-glucose disaccharide), polynucleotides encodingthese polypeptides, and methods of making and using thesepolynucleotides and polypeptides. In one embodiment, the inventionprovides thermostable and thermotolerant forms of polypeptides of theinvention. The polypeptides and nucleic acids of the invention are usedin a variety of pharmaceutical, agricultural and industrial contexts;for example, as enzymes for the bioconversion of a biomass, e.g.,lignocellulosic residues, into fermentable sugars, where in one aspectthese sugars are used as a chemical feedstock for the production ofethanol and fuels, e.g., biofuels, e.g., synthetic liquid or gas fuels,including ethanol, methanol and the like.

3. BACKGROUND

There is a great interest in the bioconversion of biomass, such asmaterial comprising lignocellulosic residues, into fermentable sugars.These sugars can be used in turn as chemical feedstock for theproduction of a biofuel, which is a clean-burning renewable energysource. Accordingly, there is a need in the industry for non-chemicalmeans for processing biomass to make clean-burning renewable fuels.

4. SUMMARY OF THE INVENTION

The present disclosure provides variant CBH I polypeptides comprising atleast one amino acid substitution as compared to BD29555. “Variant”means a polypeptide that differs in sequence from BD29555 bysubstitution of one or more amino acids at one or a number of differentsites in the amino acid sequence.

CBH I belong to the glycosyl hydrolase family 7 (“GH7”). Thecellobiohydrolases of this family, which includes endoglucanases andcellobiohydrolases, act processively from the reducing ends of cellulosechains to generate cellobiose. Cellulases of bacterial and fungal origincharacteristically have a small cellulose-binding domain (“CBD”)connected to either the N or the C terminus of the catalytic domain(“CD”) via a linker peptide (see Suumakki et al., 2000, Cellulose 7:189-209). The CD contains the active site whereas the CBD interacts withcellulose by binding the enzyme to it (van Tilbeurgh et al., 1986, FEBSLett. 204(2): 223-227; Tomme et al., 1988, Eur. J. Biochem.170:575-581). The three-dimensional structure of the catalytic domain ofT. reesei CBH I has been solved (Divne et al., 1994, Science265:524-528). The CD consists of two β-sheets that pack face-to-face toform a β-sandwich. Most of the remaining amino acids in the CD are loopsconnecting the β-sheets. Some loops are elongated and bend around theactive site, forming cellulose-binding tunnel of (˜50 Å). Typically, thecatalytic residues are glumates corresponding to E234 and E239 ofBD29555. The loop characteristic of the active site (“the active siteloops”) of CBH I polypeptides, which are absent from GH7 familyendoglucanases, corresponds to positions 214-226 of BD29555 (SEQ IDNO:134).

Many CBH I polypeptides do not have a CBD, and most studies concerningthe activity of cellulase domains on different substrates have beencarried out with only the catalytic domains of CBH I polypeptides.Because CDs with cellobiohydrolase activity can be generated by limitedproteolysis of mature CBH I by papain (see, e.g., Chen et al., 1993,Biochem. Mol. Biol. Int. 30(5):901-10), they are often referred to as“core” domains. Accordingly, a variant BD29555 can include only a CD“core”, which corresponds to positions 26-455 of SEQ ID NO:134.

The catalytic residues in the CD of BD29555, E234 and E239, are highlyconserved. Accordingly, the CBH I variants of the disclosure preferablycontain two glutamic acid residues at the positions corresponding toE234 and E239 Amino acid positions in the BD29555 variants (e.g., thosethat include an insertion or deletion) that correspond to E234 and E239can be identified through alignment of their sequences with BD29555using a sequence comparison algorithm Optimal alignment of sequences forcomparison can be conducted, e.g., by the local homology algorithm ofSmith & Waterman, 1981, Adv. Appl. Math. 2:482-89; by the homologyalignment algorithm of Needleman & Wunsch, 1970, J. Mol. Biol.48:443-53; by the search for similarity method of Pearson & Lipman,1988, Proc. Nat'l Acad. Sci. USA 85:2444-48, by computerizedimplementations of these algorithms (GAP, BESTFIT, FASTA, and TFASTA inthe Wisconsin Genetics Software Package, Genetics Computer Group, 575Science Dr., Madison, Wis.), or by visual inspection.

The CBDs are particularly involved in the hydrolysis of crystallinecellulose. It has been shown that the ability of cellobiohydrolases todegrade crystalline cellulose decreases when the CBD is absent (Linderand Teeri, 1997, Journal of Biotechnol. 57:15-28). The variant CBH Ipolypeptides of the disclosure can further include a CBD. The CBD ofBD29555 corresponds to positions 494 to 529 of SEQ ID NO:134.

The CD and CBD of a CBH I polypeptide are often connected via a linker.The CBD can be N- or C-terminal to the CD, and the CBD and CD areoptionally connected via a linker sequence. The linker connecting the CDand CBD of BD29555 corresponds to positions 456 to 493 of SEQ ID NO:134.

Because CBH I polypeptides are modular, a CD variant of BD29555 can becombined with a CBD and/or linkers of a different CBH I polypeptide. Inone embodiment, however, a variant CBH I polypeptide comprises a CD, CBDand linker that are related in sequence to BD29555.

Most CBH I polypeptides are secreted and are therefore expressed with asignal sequence that is cleaved upon secretion of the polypeptide fromthe cell. The variant CBH I polypeptides of the disclosure can be maturepolypeptides or they may further comprise a signal sequence. The matureBD29555 corresponds to amino acids 26 to 529 of SEQ ID NO:134, and thesignal sequence of BD29555 corresponds to amino acids 1 to 25 of SEQ IDNO:134. The variant CBH I polypeptides of the disclosure can beexpressed with the signal sequence of BD29555, or with a heterologoussignal sequence.

The variant CBH I polypeptides have at least one improved property(e.g., activity, improved thermotolerance, improved product tolerance)as compared to wild type BD29555 (whose sequence is provided as SEQ IDNO:60, 94, 120 or 134). Table A provides a summary of substitutions thatcan be introduced into a BD29555 polypeptide:

TABLE A Sequence Identifier Location of (SEQ ID NO:) Substitution(s)Substitution(s) Improvement 2 N222H CD (active site loop) Activity 4N222E CD (active site loop) Activity 6 S217K CD (active site loop)Activity 8 L225Y CD (active site loop) Activity 10 L225V CD (active siteloop) Activity 12 H497S CBD Activity 14 T510K CBD Activity 16 D87L CDActivity 18 G256I CD Activity 20 H157G CD Activity 22 P159G CD Activity24 N183A CD Activity 26 S156G CD Activity 28 S218P, T316S S218P: CD(active site loop) Activity T316S: CD 30 D318Q, T322S, I363V CD Activity32 T324R CD Activity 34 S326L CD Activity 36 Q334S CD Activity 38 K345DCD Activity 40 K45R, T293A, S350C CD Activity 42 G351D CD Activity 44N352V CD Activity 46 F358L CD Activity 48 A370I CD Activity 50 G376R CDActivity 52 E386S CD Activity 54 V451W CD Activity 56 N455G CD Activity58 S463K Linker Activity 60 S104N CD Thermotolerance 64 V121S CDThermotolerance 66 V121T CD Thermotolerance 68 G113N CD Thermotolerance70 L116T CD Thermotolerance 72 T268V CD Thermotolerance 74 T35A, V401ACD Thermotolerance 76 V392T CD Thermotolerance 78 Y399D CDThermotolerance 80 V401D CD Thermotolerance 82 V392A, V401A, T417A CDThermotolerance 84 L404T CD Thermotolerance 86 S463Y CD Thermotolerance88 A221V, V401A, G474W A221V: CD (active site loop) ThermotoleranceV401A, G474W: CD 90 A472M Linker Thermotolerance 92 V401A, V494L V401A:CD Thermotolerance V494L: CBD 96 Y31L, T32Q, S72A, T73Q, T77D, CDActivity F120-VTGSNVG-S128 → F120-VQQGPYSKNVG-S132 98 Y31L, S72W, T77D,CD Activity F120-VTGSNVG-S128 → F120-VQQGPYSKNVG-S132 100 S72Y, T73Q, CDActivity F120-VTGSNVG-S128 → F120-VQQGPYSKNVG-S132 102 Y31L, T32W, CDActivity F120-VTGSNVG-S128 → F120-VQQGPYSKNVG-S132 104 T32Q, CD ActivityF120-VTGSNVG-S128 → F120-VTKGSFSSNIG-S132 106 Y31Q, T32Q, S72Y, T77D, CDActivity F120-VTGSNVG-S128 → F120-VTQSAQKNVG-A131 108 Y31A, T32Y, S72Y,T73Y, T77D CD Activity 110 Y31Q, T32Q, S72Y, T73Y, T77D CD Activity 112T32W, T73W, T77D CD Activity 114 Y31A, T32Q, T73Y, T77D CD Activity 116S72W, T73Q, CD Activity F120-VTGSNVG-S128 → F120-VQQGPYSKNVG-S132 118Y31L, T32Y, T77D, CD Activity F120-VTGSNVG-S128 → F120-VQQGPYSKNVG-S132122 P159G, S217K, N222H, L225Y, P159G, K345D, N352V, V451W: CD ActivityK345D, N352V, V451W S217K, N222H, L225Y: CD (active site loop) 124N222H, L225Y, K345D, N352V, K345D, N352V, E386S, V451W: CD ActivityE386S, V451W N222H, L225Y: CD (active site loop) 126 S326L, K345D, N352VCD Activity 128 L225Y, D318Q, T324R, S326L, D318Q, T324R, S326L, K345D,E386S: CD Activity K345D, E386S L225Y: CD (active site loop) 130 P159G,S217K, N222H, L225Y, P159G, Q334S, K345D, E386S: CD Activity Q334S,K345D, E386S S217K, N222H, L225Y: CD (active site loop) 132 E386S, V451WCD Activity 136 R273K, R422K CD Product Tolerance

Accordingly, the present disclosure provides CBH I variant polypeptideshaving improved activity relative to BD29555, which have one or more thefollowing substitutions or combinations of substitutitions as comparedto the BD29555 sequence (SEQ ID NO:134): (a) N222H; (b) N222E; (c)S217K; (d) L225Y; (e) L225V; (f) H497S; (g) T510K; (h) D87L; (i) G256I;(j) H157G; (k) P159G; (l) N183A; (m) S156G; (n) S218P+T316S; (o)D318Q+T322S+1363V; (p) T324R; (q) S326L; (r) Q334S; (t) K345D; (u)K45R+T293A+S350C; (v) G351D; (w) N352V; (x) F358L; (y) A370I; (z) G376R;(aa) E386S; (bb) V451W; (cc) N455G; (dd) S463K; (ee)Y31L+T32Q+S72A+T73Q+T77D+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (ff)Y31L+S72W+T77D+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (gg)S72Y+T73Q+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (hh)Y31L+T32W+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (ii)T32Q+F120-VTGSNVG-S128→F120-VTKGSFSSNIG-S132; (jj)Y31Q+T32Q+S72Y+T77D+F120-VTGSNVG-S128→F120-VTQSAQKNVG-A131; (kk)Y31A+T32Y+S72Y+T73Y+T77D; (11) Y31Q+T32Q+S72Y+T73Y+T77D; (mm)T32W+T73W+T77D; (nn) Y31A+T32Q+T73Y+T77D; (oo)S72W+T73Q+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (pp)Y31L+T32Y+T77D+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (qq)P159G+S217K+N222H+L225Y+K345D+N352V+V451W; (a)N222H+L225Y+K345D+N352V+E386S+V451W; (ss) S326L+K345D+N352V; (tt)L225Y+D318Q+T324R+S326L+K345D+E386S; (uu)P159G+S217K+N222H+L225Y+Q334S+K345D+E386S; (vv) E386S+V451W.

The present disclosure also provides CBH I variant polypeptides havingimproved thermal tolerance relative to BD29555, which have one or morethe following substitutions or combinations of substitutitions ascompared to the BD29555 sequence (SEQ ID NO:134(a) S104N; (b) V121S; (c)V121T; (d) G113N; (e) L116T; (f) T268V; (g) T35A+V401A; (h) V392T; (i)Y399D; (j) V401D; (k) V392A+V401A+T417A; (l) L404T; (m) S463Y; (n)A221V+V401A+G474W; (o) A472M; (p) V401A+V494L.

BD29555 has a surface loop at amino acid positions 120-128, whichtogether with positions 31, 32, 72, 73, and 77, forms the substrateentry site. A “substrate entry site” library with 12,800 variants wasconstructed with the aim to increase the hydrophobicity of the entrysite for improved substrate uptake (the library contained 5 variants atposition 31, and 4 variants each at positions 32, 72, 73, and 77; inaddition, nine loops of various lengths and amino acid compositions fromother CBH I sequences substituted the surface loop at positions120-128). Several variants with improved activity were identified in thesubstrate entry site screen (corresponding to SEQ ID NOs:96, 98, 100,102, 104, 106, 108, 110, 112, 114, 116 and 118. Additionally, SEQ IDNO:64 and SEQ ID NO:66 represent BD29555 variants with beneficialsubstitutions in the substrate entry site that were identified in otherscreens that improved the enzyme's thermal tolerance. Accordingly, incertain aspects, the present disclosure provides substrate entry sitevariants of BD29555 that increase CBH I activity or thermal tolerance.In some embodiments, the substrate entry site variants include one ormore substitutions or combinations of substitutions selected from: (a)V121S; (b) V121T; (c)Y31L+T32Q+S72A+T73Q+T77D+F120-VTGSNVG-5128→F120-VQQGPYSKNVG-S132; (d)Y31L+S72W+T77D+F120-VTGSNVG-5128→F120-VQQGPYSKNVG-S132; (e)S72Y+T73Q+F120-VTGSNVG-5128→F120-VQQGPYSKNVG-S132; (f)Y31L+T32W+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (g)T32Q+F120-VTGSNVG-5128→F120-VTKGSFSSNIG-S132; (g)Y31Q+T32Q+S72Y+T77D+F120-VTGSNVG-5128→F120-VTQSAQKNVG-A131; (h)Y31A+T32Y+S72Y+T73Y+T77D; (i) Y31Q+T32Q+S72Y+T73Y+T77D; (j)T32W+T73W+T77D; (k) Y31A+T32Q+T73Y+T77D; (l)S72W+T73Q+F120-VTGSNVG-5128→F120-VQQGPYSKNVG-S132; and (m)Y31L+T32Y+T77D+F120-VTGSNVG-5128→F120-VQQGPYSKNVG-S132. It is notedthat, as used herein in the context of the surface loop present atpositions of 120-128, the term substitutions refers to eithersubstitution of one or more individual amino acids or substitution ofthe entire loop (9 amino acids) with a loop of different length (e.g.,6, 7, 8, 10, 11, 12, 13, 14 or 15 amino acids).

The CBH I polypeptides of the disclosure comprise an amino acid sequencehaving at least 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%,61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%,75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%,89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 99.5% sequenceidentity to the CD of BD29555. The sequence of BD29555 is set forth asSEQ ID NO:60, 94, 120 and 134. The CD of BD29555 corresponds topositions 26-455 of SEQ ID NO:60, 94, 120 or 134.

The CBH I polypeptides of the disclosure can also comprise an amino acidsequence having at least 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%,59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%,73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%,87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 99.5%sequence identity to the mature polypeptide resulting from cleavage ofthe signal sequence of BD29555. The sequence of BD29555 is set forth asSEQ ID NO:60, 94, 120 and 134. The mature polypeptide corresponds topositions 26-529 of SEQ ID NO:60, 94, 120 or 134.

The present disclosure further provides compositions (includingcellulase compositions, e.g., whole cellulase compositions, andfermentation broths) comprising variant CBH I polypeptides. The variantCBH I polypeptides and compositions comprising them can be used, interalia, in processes for saccharifying biomass.

The present disclosure further provides nucleic acids (e.g., vectors)comprising nucleotide sequences encoding variant CBH I polypeptides asdescribed herein, and recombinant cells engineered to express thevariant CBH I polypeptides. The recombinant cell can be a prokaryotic(e.g., bacterial) or eukaryotic (e.g., yeast or filamentous fungal)cell. Further provided are methods of producing and optionallyrecovering the variant CBH I polypeptides.

In alternative embodiments, the invention provides polypeptides havinglignocellulolytic (lignocellulosic) activity, e.g., a ligninolytic andcellulolytic activity, including, e.g., having cellulase, endoglucanase,cellobiohydrolase (cbhl) (e.g., an exo-cellobiohydrolase, e.g., havingan “exo” activity that can processively release cellobiose units (β-1,4glucose-glucose disaccharide), β-glucosidase (beta-glucosidase),xylanase, xylosidase (e.g., β-xylosidase), and/or an arabinofuranosidaseactivity, and nucleic acids encoding them, and methods for making andusing them. The invention provides enzymes for the bioconversion of anybiomass, e.g., a lignocellulosic residue, into fermentable sugars orpolysaccharides; and these sugars or polysaccharides can be used as achemical feedstock for the production of alcohols such as ethanol,propanol, butanol and/or methanol, and in the production of fuels, e.g.,biofuels such as synthetic liquids or gases, such as syngas.

In alternative embodiments, the enzymes of the invention have anincreased catalytic rate to improve the process of substrate (e.g., alignocellulosic residue, cellulose, bagasse) hydrolysis. This increasedefficiency in catalytic rate leads to an increased efficiency inproducing sugars or polysaccharides, which can be useful in industrial,agricultural or medical applications, e.g., to make a biofuel or analcohol such as ethanol, propanol, butanol and/or methanol. In oneaspect, sugars produced by hydrolysis using enzymes of this inventioncan be used by microorganisms for alcohol (e.g., ethanol, propanol,butanol and/or methanol) production and/or fuel (e.g., biofuel)production.

In alternative embodiments, the invention provides highly activepolypeptides having lignocellulosic activity, e.g., polypeptides havingan increased catalytic rate that include glycosyl hydrolases,endoglucanases, cellobiohydrolases (cbhl) (e.g., exo-cellobiohydrolases,e.g., having an “exo” activity that can processively release cellobioseunits β-1,4 glucose-glucose disaccharide), β-glucosidases(beta-glucosidases), xylanases, xylosidase (e.g., β-xylosidase) and/orarabinofuranosidases.

In alternative embodiments, the invention provides industrial,agricultural or medical applications: e.g., biomass to biofuel, e.g.,ethanol, propanol, butanol and/or methanol, using enzymes of theinvention having decreased enzyme costs, e.g., decreased costs inbiomass to biofuel conversion processes. Thus, the invention providesefficient processes for producing bioalcohols, biofuels and/or biofuel-(e.g., bioethanol-, propanol-, butanol- and/or methanol-) comprisingcompositions, including synthetic, liquid or gas fuels comprising abioalcohol, from any biomass.

In alternative embodiments, enzymes of the invention, including theenzyme “cocktails” of the invention (“cocktails” meaning mixtures ofenzymes comprising at least one enzyme of this invention), are used tohydrolyze the major components of a lignocellulosic biomass, or anycomposition comprising cellulose and/or hemicellulose (lignocellulosicbiomass also comprises lignin), e.g., seeds, grains, tubers, plant waste(such as a hay or straw, e.g., a rice straw or a wheat straw, or any thedry stalk of any cereal plant) or byproducts of food processing orindustrial processing (e.g., stalks), corn (including cobs, stover, andthe like), grasses (e.g., Indian grass, such as Sorghastrum nutans; or,switch grass, e.g., Panicum species, such as Panicum virgatum), wood(including wood chips, processing waste, such as wood waste), paper,pulp, recycled paper (e.g., newspaper); also including a monocot or adicot, or a monocot corn, sugarcane or parts thereof (e.g., cane tops),rice, wheat, barley, switchgrass or Miscanthus; or a dicot oilseed crop,soy, canola, rapeseed, flax, cotton, palm oil, sugar beet, peanut, tree,poplar or lupine.

In alternative embodiments, enzymes of the invention are used tohydrolyze cellulose comprising a linear chain of β-1,4-linked glucosemoieties, and/or hemicellulose as a complex structure that varies fromplant to plant. In one aspect, enzymes of the invention are used tohydrolyze hemicelluloses containing a backbone of β-1,4 linked xylosemolecules with intermittent branches of arabinose, galactose, glucuronicacid and/or mannose. In one aspect, enzymes of the invention are used tohydrolyze hemicellulose containing non-carbohydrate constituents such asacetyl groups on xylose and ferulic acid esters on arabinose. In oneaspect, enzymes of the invention are used to hydrolyze hemicellulosescovalently linked to lignin and/or coupled to other hemicellulosestrands via diferulate crosslinks.

In alternative embodiments, the compositions and methods of theinvention are used in the enzymatic digestion of biomass and cancomprise use of many different enzymes, including the cellulases andhemicellulases. Lignocellulosic enzymes used to practice the inventioncan digest cellulose to monomeric sugars, including glucose. In oneaspect, compositions used to practice the invention can include mixturesof enzymes, e.g., glycosyl hydrolases, glucose oxidases, xylanases,xylosidases (e.g., β-xylosidases), cellobiohydrolases (cbhl) (e.g.,exo-cellobiohydrolases, e.g., having an “exo” activity that canprocessively release cellobiose units β-1,4 glucose-glucosedisaccharide) and/or arabinofuranosidases or other enzymes that candigest hemicellulose to monomer sugars. Mixtures of the invention cancomprise, or consist of, only enzymes of this invention, or can includeat least one enzyme of this invention and another enzyme, which can alsobe a lignocellulosic enzyme and/or any other enzyme, e.g., a glucoseoxidase.

In alternative embodiments, compositions used to practice the inventioninclude a “cellulase” or composition that is a mixture of at least threedifferent enzyme types (or an enzyme having more than one enzymaticproperty): (1) an endoglucanase, which cleaves internal β-1,4 linkagesresulting in shorter glucooligosaccharides, (2) a cellobiohydrolase,which can act in an “exo” manner processively releasing cellobiose units(β-1,4 glucose-glucose disaccharide), and (3) a β-glucosidase, releasingglucose monomer from short cellooligosaccharides (e.g. cellobiose); or acomposition comprising one, two or all three of these enzyme types orenzyme activities.

In alternative embodiments, the enzymes of the invention have aglucanase, e.g., an endoglucanase, activity, e.g., catalyzing hydrolysisof internal endo-β-1,4- and/or β-1,3-glucanase linkages. In one aspect,the endoglucanase activity (e.g., endo-1,4-beta-D-glucan 4-glucanohydrolase activity) comprises hydrolysis of 1,4- and/orβ-1,3-beta-D-glycosidic linkages in cellulose, cellulose derivatives(e.g., carboxy methyl cellulose and hydroxy ethyl cellulose) lichenin,beta-1,4 bonds in mixed beta-1,3 glucans, such as cereal beta-D-glucansor xyloglucans and other plant material containing cellulosic parts.

In alternative embodiments, enzymes of the invention have endoglucanase(e.g., endo-beta-1,4-glucanases, EC 3.2.1.4;endo-beta-1,3(1)-glucanases, EC 3.2.1.6; endo-beta-1,3-glucanases, EC3.2.1.39) activity and can hydrolyze internal β-1,4- and/orβ-1,3-glucosidic linkages in cellulose and glucan to produce smallermolecular weight glucose and glucose oligomers. The invention providesmethods for producing smaller molecular weight glucose and glucoseoligomers using these enzymes of the invention.

In alternative embodiments, enzymes of the invention are used togenerate glucans, e.g., polysaccharides formed from 1,4-β- and/or1,3-glycoside-linked D-glucopyranose. In one aspect, the endoglucanasesof the invention are used in the food industry, e.g., for baking andfruit and vegetable processing, breakdown of agricultural waste, in themanufacture of animal feed, in pulp and paper production, textilemanufacture and household and industrial cleaning agents. In one aspect,the enzymes, e.g., endoglucanases, of the invention are produced by amicroorganism, e.g., by a fungi and/or a bacteria.

In alternative embodiments, enzymes, e.g., endoglucanases, of theinvention are used to hydrolyze beta-glucans (β-glucans) which are majornon-starch polysaccharides of cereals. The glucan content of apolysaccharide can vary significantly depending on variety and growthconditions. The physicochemical properties of this polysaccharide aresuch that it gives rise to viscous solutions or even gels underoxidative conditions. In addition glucans have high water-bindingcapacity. All of these characteristics present problems for severalindustries including brewing, baking, animal nutrition. In brewingapplications, the presence of glucan results in wort filterability andhaze formation issues. In baking applications (especially for cookiesand crackers), glucans can create sticky doughs that are difficult tomachine and reduce biscuit size. Thus, the enzymes, e.g.,endoglucanases, of the invention are used to decrease the amount ofβ-glucan in a β-glucan-comprising composition, e.g., enzymes of theinvention are used in processes to decrease the viscosity of solutionsor gels; to decrease the water-binding capacity of a composition, e.g.,a β-glucan-comprising composition; in brewing processes (e.g., toincrease wort filterability and decrease haze formation), to decreasethe stickiness of doughs, e.g., those for making cookies, breads,biscuits and the like.

In alternative embodiments, enzymes, e.g., endoglucanases, of theinvention are used to retain crispiness, increase crispiness, or reducethe rate of loss of crispiness, and to increase the shelf-life of anycarbohydrate-comprising food, feed or drink, e.g., a β-glucan-comprisingfood, feed or drink. In alternative embodiments, enzymes, e.g.,endoglucanases, of the invention are used to decrease the amount ofcarbohydrates (e.g., β-glucan) implicated in rapid rehydration of bakedproducts and other food or baked products resulting in loss ofcrispiness and reduced shelf-life.

In alternative embodiments, enzymes, e.g., endoglucanases, of theinvention are used to decrease the viscosity of gut contents (e.g., inanimals, such as ruminant animals, or humans), e.g., those with cerealdiets. Thus, in alternative aspects, enzymes, e.g., endoglucanases, ofthe invention are used to positively affect the digestibility of a foodor feed and animal (e.g., human or domestic animal) growth rate, and inone aspect, are used to higher generate feed conversion efficiencies.For monogastric animal feed applications with cereal diets, beta-glucanis a contributing factor to viscosity of gut contents and therebyadversely affects the digestibility of the feed and animal growth rate.For ruminant animals, these beta-glucans represent substantialcomponents of fiber intake and more complete digestion of glucans wouldfacilitate higher feed conversion efficiencies. Accordingly, theinvention provides animal feeds and foods comprising endoglucanases ofthe invention, and in one aspect, these enzymes are active in an animaldigestive tract, e.g., in a stomach and/or intestine.

In alternative embodiments, enzymes of the invention are used to digestcellulose or any beta-1,4-linked glucan-comprising synthetic or naturalmaterial, including those found in any plant material. Enzymes, e.g.,endoglucanases, of the invention are used as commercial enzymes todigest cellulose from any source, including all biological sources, suchas plant biomasses, e.g., corn, grains, grasses (e.g., Indian grass,such as Sorghastrum nutans; or, switch grass, e.g., Panicum species,such as Panicum virgatum); also including a monocot or a dicot, or amonocot corn, sugarcane or parts thereof (e.g., cane tops), rice, wheat,barley, switchgrass or Miscanthus; or a dicot oilseed crop, soy, canola,rapeseed, flax, cotton, palm oil, sugar beet, peanut, tree, poplar orlupine; or, woods or wood processing byproducts, such as wood waste,e.g., in the wood processing, pulp and/or paper industry, in textilemanufacture and in household and industrial cleaning agents, and/or inbiomass waste processing.

In alternative embodiments, the invention provides compositions (e.g.,pharmaceutical compositions, foods, feeds, drugs, dietary supplements)comprising the enzymes, polypeptides or polynucleotides of theinvention. These compositions can be formulated in a variety of forms,e.g., as pills, capsules, tablets, gels, geltabs, lotions, pills,injectables, implants, liquids, sprays, powders, food, additives,supplements, feed or feed pellets, or as any type of encapsulated form,or any type of formulation.

The invention provides isolated, synthetic or recombinant nucleic acidscomprising a nucleic acid sequence having at least about 50%, 51%, 52%,53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%,67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%,81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%,95%, 96%, 97%, 98%, 99%, or more, or complete (100%) sequence identity(homology) to an exemplary nucleic acid of the invention, including SEQID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ IDNO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ IDNO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ IDNO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ IDNO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ IDNO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ IDNO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ ID NO:69, SEQ IDNO:71, SEQ ID NO:73, SEQ ID NO:75, SEQ ID NO:77, SEQ ID NO:79, SEQ IDNO:81, SEQ ID NO:83, SEQ ID NO:85, SEQ ID NO:87, SEQ ID NO:89, SEQ IDNO:91, SEQ ID NO:93, SEQ ID NO:95, SEQ ID NO:97, SEQ ID NO:99, SEQ IDNO:101, SEQ ID NO:103, SEQ ID NO:105, SEQ ID NO:107, SEQ ID NO:109, SEQID NO:111, SEQ ID NO:113, SEQ ID NO:115, SEQ ID NO:117, SEQ ID NO:119,SEQ ID NO:121, SEQ ID NO:123, SEQ ID NO:125, SEQ ID NO:127, SEQ IDNO:129, SEQ ID NO:131, SEQ ID NO:133, and/or SEQ ID NO:135; which inalternative embodiments include complementary (partially or completelycomplementary) (e.g., antisense) sequence, cDNA coding sequences andgenomic (e.g., “gDNA”) sequences, and optionally include sequences overa region of at least about 10, 15, 20, 25, 30, 35, 40, 45, 50, 75, 100,150, 200, 250, 300, 350, 400, 450, 500, 550, 600, 650, 700, 750, 800,850, 900, 950, 1000, 1050, 1100, 1150, 1200, 1250, 1300, 1350, 1400,1450, 1500, 1550, 1600, 1650, 1700, 1750, 1800, 1850, 1900, 1950, 2000,2050, 2100, 2200, 2250, 2300, 2350, 2400, 2450, 2500, or more residues;or over a region consisting of the protein coding region (e.g., thecDNA) or the genomic sequence; and all of these nucleic acid sequences,and the polypeptides and peptides they encode, encompass “sequences ofthe invention”.

In alternative aspects, these nucleic acids of the invention encode atleast one polypeptide having a lignocellulolytic activity, e.g., acellulase or a cellobiohydrolase (e.g., a cbhl) (e.g., anexo-cellobiohydrolase, e.g., having an “exo” activity that canprocessively release cellobiose units β-1,4 glucose-glucosedisaccharide) activity. In alternative embodiments, a nucleic acid ofthe invention can encode a polypeptide capable of generating an antibody(or any binding fragment thereof) that can specifically bind to anexemplary polypeptide of the invention (listed below), or, these nucleicacids can be used as probes for identifying or isolating lignocelluloticenzyme-encoding nucleic acids, or to inhibit the expression oflignocellulotic enzyme-expressing nucleic acids (all these aspectsreferred to as the “nucleic acids of the invention”). In one aspect, thesequence identities are determined by analysis with a sequencecomparison algorithm or by a visual inspection.

Nucleic acids of the invention also include isolated, synthetic orrecombinant nucleic acids encoding an exemplary polypeptide (or peptide)of the invention which include polypeptides (e.g., enzymes) of theinvention having the sequence of (or the subsequences of, orenzymatically active fragments of) SEQ ID NO:2, SEQ ID NO:4, SEQ IDNO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ IDNO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ IDNO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ IDNO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ IDNO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ IDNO:56, SEQ ID NO:58; SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ IDNO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:72, SEQ ID NO:74, SEQ IDNO:76, SEQ ID NO:78, SEQ ID NO:80, SEQ ID NO:82, SEQ ID NO:84, SEQ IDNO:86, SEQ ID NO:88, SEQ ID NO:90, SEQ ID NO:92, SEQ ID NO:94, SEQ IDNO:96, SEQ ID NO:98, SEQ ID NO:100, SEQ ID NO:102, SEQ ID NO:104, SEQ IDNO:106, SEQ ID NO:108, SEQ ID NO:110, SEQ ID NO:112, SEQ ID NO:114, SEQID NO:116, SEQ ID NO:118, SEQ ID NO:120, SEQ ID NO:122, SEQ ID NO:124,SEQ ID NO:126, SEQ ID NO:128, SEQ ID NO:130, SEQ ID NO:132, SEQ IDNO:134, and/or SEQ ID NO:136.

Alternative embodiments of the invention comprise isolated, synthetic orrecombinant nucleic acids including at least 10, 15, 20, 25, 30, 35, 40,45, 50, 75, 100, 150, 200, 250, 300, 350, 400, 450, 500, 550, 600, 650,700, 750, 800, 850, 900, 950, 1000, 1050, 1100, 1150, 1200, 1250, 1300,1350, 1400, 1450, 1500, 1550, 1600, 1650, 1700, 1750, 1800, 1850, 1900,1950, 2000, 2050, 2100, 2200, 2250, 2300, 2350, 2400, 2450, 2500, ormore consecutive bases of a nucleic acid sequence of the invention,sequences substantially identical thereto, and the sequences (partiallyor completely) complementary thereto.

In alternative embodiments, isolated, synthetic or recombinant nucleicacids of the invention encode a polypeptide having a lignocellulosicactivity, e.g., cellulase or cellobiohydrolase activity, which isthermostable. The polypeptide can retain a lignocellulosic activityunder conditions comprising a temperature range of between about 37° C.to about 95° C.; between about 55° C. to about 85° C., between about 70°C. to about 95° C., or, between about 90° C. to about 95° C. Thepolypeptide can retain a lignocellulosic activity in temperatures in therange between about 1° C. to about 5° C., between about 5° C. to about15° C., between about 15° C. to about 25° C., between about 25° C. toabout 37° C., between about 37° C. to about 95° C., 96° C., 97° C., 98°C. or 99° C., between about 55° C. to about 85° C., between about 70° C.to about 75° C., or between about 90° C. to about 99° C., or 95° C., 96°C., 97° C., 98° C. or 99° C., or more.

In alternative embodiments, isolated, synthetic or recombinant nucleicacids of the invention encode a polypeptide having a lignocellulosicactivity, e.g., cellulase or cellobiohydrolase activity, that canhydrolyze (degrade) soluble cellooligsaccharides into monomers, which isthermotolerant. The polypeptide can retain a lignocellulosic activity orcellulase or cellobiohydrolase activity after exposure to a temperaturein the range from greater than 37° C. to about 95° C. or anywhere in therange from greater than 55° C. to about 85° C. The polypeptide canretain a lignocellulosic activity after exposure to a temperature in therange between about 1° C. to about 5° C., between about 5° C. to about15° C., between about 15° C. to about 25° C., between about 25° C. toabout 37° C., between about 37° C. to about 95° C., 96° C., 97° C., 98°C. or 99° C., between about 55° C. to about 85° C., between about 70° C.to about 75° C., or between about 90° C. to about 95° C., or more. Inone aspect, the polypeptide retains a lignocellulosic activity afterexposure to a temperature in the range from greater than 90° C. to about99° C., or 95° C., 96° C., 97° C., 98° C. or 99° C., at about pH 4.5, ormore.

In alternative embodiments the invention provides a nucleic acid probefor identifying or isolating a nucleic acid encoding a polypeptidehaving a lignocellulosic activity, or can hydrolyze (degrade) solublesaccharides or oligomers into monomers, wherein the probe comprises anucleic acid comprising a sequence at least about 10, 15, 20, 30, 40,50, 60, 70, 80, 90, 100, 150, 200, 250, 300, 350, 400, 450, 500, 550,600, 650, 700, 750, 800, 850, 900, 950, 1000 or more residues of anucleic acid of the invention, e.g., a polynucleotide having at leastabout 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%,63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%,77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%,91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or more, or complete (100%)sequence identity to an exemplary nucleic acid of the invention. In oneaspect, the sequence identities are determined by analysis with asequence comparison algorithm or by visual inspection. In alternativeaspects, the probe can comprise an oligonucleotide comprising at leastabout 10 to 50, about 20 to 60, about 30 to 70, about 40 to 80, or about60 to 100 consecutive bases of a nucleic acid sequence of the invention,or a subsequence thereof.

In alternative embodiments the invention provides an amplificationprimer pair for amplifying (e.g., by PCR) a nucleic acid encoding apolypeptide having a lignocellulosic activity, e.g., a cellulase orcellobiohydrolase, or can hydrolyze (degrade) soluble oligsaccharidesand oligomers into monomers, wherein the primer pair is capable ofamplifying a nucleic acid comprising a sequence of the invention, orfragments or subsequences thereof. One or each member of theamplification primer sequence pair can comprise an oligonucleotidecomprising at least about 10 to 50, or more, consecutive bases of thesequence, or about 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22,23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36 or moreconsecutive bases of the sequence. The invention provides amplificationprimer pairs, wherein the primer pair comprises a first member having asequence as set forth by about the first (the 5′) 12, 13, 14, 15, 16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34,35, 36 or more residues of a nucleic acid of the invention, and a secondmember having a sequence as set forth by about the first (the 5′) 12,13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30,31, 32, 33, 34, 35, 36 or more residues of the complementary strand ofthe first member.

In alternative embodiments the invention providescellobiohydrolase-encoding and cellulase-encoding nucleic acids, e.g.,generated by amplification, e.g., polymerase chain reaction (PCR), usingan amplification primer pair of the invention. The invention providescellulase-encoding, e.g., cellobiohydrolase, generated by amplification,e.g., polymerase chain reaction (PCR), using an amplification primerpair of the invention. The invention provides methods of making nucleicacid encoding an enzyme with lignocellulosic activity, e.g., acellobiohydrolase, by amplification, e.g., polymerase chain reaction(PCR), using an amplification primer pair of the invention. In oneaspect, the amplification primer pair amplifies a nucleic acid from alibrary, e.g., a gene library, such as an environmental library.

In alternative embodiments the invention provides methods of amplifyinga nucleic acid encoding a polypeptide having a lignocellulosic activity,e.g., a cellobiohydrolase, or can hydrolyze (degrade) solublesaccharides and/or oligomers into monomers, comprising amplification ofa template nucleic acid with an amplification primer sequence paircapable of amplifying a nucleic acid sequence of the invention, orfragments or subsequences thereof.

In alternative embodiments the invention provides expression cassettescomprising a nucleic acid of the invention or a subsequence thereof. Inone aspect, the expression cassette can comprise the nucleic acid thatis operably linked to a promoter. The promoter can be a viral,bacterial, mammalian or plant promoter. In one aspect, the plantpromoter can be a potato, rice, corn, wheat, tobacco or barley promoter.The promoter can be a constitutive promoter. The constitutive promotercan comprise CaMV35S. In another aspect, the promoter can be aninducible promoter. In one aspect, the promoter can be a tissue-specificpromoter or an environmentally regulated or a developmentally regulatedpromoter. Thus, the promoter can be, e.g., a seed-specific, aleaf-specific, a root-specific, a stem-specific or an abscission-inducedpromoter. In one aspect, a nucleic acid of the invention encoding anendogenous or heterologous signal sequence (see discussion, below) isexpressed using an inducible promoter, an environmentally regulated or adevelopmentally regulated promoter, a tissue-specific promoter and thelike. In alternative aspects, the promoter comprises a seed preferredpromoter, such as e.g., the maize gamma zein promoter or the maizeADP-gpp promoter. In one aspect, the signal sequence targets the encodedprotein of the invention to a vacuole, the endoplasmic reticulum, thechloroplast or a starch granule.

In alternative embodiments the expression cassette can further comprisea plant or plant virus expression vector. The invention provides cloningvehicles comprising an expression cassette (e.g., a vector) of theinvention or a nucleic acid of the invention. The cloning vehicle can bea viral vector, a plasmid, a phage, a phagemid, a cosmid, a fosmid, abacteriophage or an artificial chromosome. The viral vector can comprisean adenovirus vector, a retroviral vector or an adeno-associated viralvector. The cloning vehicle can comprise a bacterial artificialchromosome (BAC), a plasmid, a bacteriophage P1-derived vector (PAC), ayeast artificial chromosome (YAC), or a mammalian artificial chromosome(MAC).

In alternative embodiments the invention provides transformed cellscomprising a nucleic acid of the invention or an expression cassette(e.g., a vector, plasmid, etc.) of the invention, or a cloning vehicle(e.g., artificial chromosome) of the invention. In one aspect, thetransformed cell can be a bacterial cell, a mammalian cell, a fungalcell, a yeast cell, an insect cell or a plant cell. In one aspect, theplant cell can be soybeans, rapeseed, oilseed, tomato, cane sugar, acereal, a potato, wheat, rice, corn, tobacco or barley cell; the plantcell also can be a monocot or a dicot, or a monocot corn, sugarcane,rice, wheat, barley, Indian grass, switchgrass or Miscanthus; or a dicotoilseed crop, soy, canola, rapeseed, flax, cotton, palm oil, sugar beet,peanut, tree, poplar or lupine.

In alternative embodiments the invention provides transgenic non-humananimals comprising a nucleic acid of the invention or an expressioncassette (e.g., a vector) of the invention. In one aspect, the animal isa mouse, a cow, a rat, a pig, a goat or a sheep.

In alternative embodiments the invention provides transgenic plantscomprising a nucleic acid of the invention or an expression cassette(e.g., a vector) of the invention. The transgenic plant can be anycereal plant, a corn plant, a potato plant, a tomato plant, a wheatplant, an oilseed plant, a rapeseed plant, a soybean plant, a riceplant, a barley plant or a tobacco plant. The transgenic plant can be amonocot or a dicot, or a monocot corn, sugarcane, rice, wheat, barley,switchgrass or Miscanthus; or a dicot oilseed crop, soy, canola,rapeseed, flax, cotton, palm oil, sugar beet, peanut, tree, poplar orlupine.

In alternative embodiments the invention provides transgenic seedscomprising a nucleic acid of the invention or an expression cassette(e.g., a vector) of the invention. The transgenic seed can be a cerealplant, a corn seed, a wheat kernel, an oilseed, a rapeseed, a soybeanseed, a palm kernel, a sunflower seed, a sesame seed, a peanut or atobacco plant seed. The transgenic seed can be derived from a monocot ora dicot, or a monocot corn, sugarcane, rice, wheat, barley, switchgrassor Miscanthus; or a dicot oilseed crop, soy, canola, rapeseed, flax,cotton, palm oil, sugar beet, peanut, tree, poplar or lupine.

In alternative embodiments the invention provides an antisenseoligonucleotide comprising a nucleic acid sequence complementary to orcapable of hybridizing under stringent conditions to a nucleic acid ofthe invention. The invention provides methods of inhibiting thetranslation of a lignocellulosic enzyme, e.g., a cellulase orcellobiohydrolase, message in a cell comprising administering to thecell or expressing in the cell an antisense oligonucleotide comprising anucleic acid sequence complementary to or capable of hybridizing understringent conditions to a nucleic acid of the invention. In one aspect,the antisense oligonucleotide is between about 10 to 50, about 20 to 60,about 30 to 70, about 40 to 80, or about 60 to 100 bases in length,e.g., 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85,90, 95, 100 or more bases in length. The invention provides methods ofinhibiting the translation of a lignocellulosic enzyme message in a cellcomprising administering to the cell or expressing in the cell anantisense oligonucleotide comprising a nucleic acid sequencecomplementary to or capable of hybridizing under stringent conditions toa nucleic acid of the invention.

In alternative embodiments the invention provides double-strandedinhibitory RNA (RNAi, or RNA interference) molecules (including smallinterfering RNA, or siRNAs, for inhibiting transcription, and microRNAs,or miRNAs, for inhibiting translation) comprising a subsequence of asequence of the invention. In one aspect, the siRNA is between about 21to 24 residues, or, about at least 15, 16, 17, 18, 19, 20, 21, 22, 23,24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 40, 45, 50, 55, 60, 65,70, 75, 80, 85, 90, 95, 100 or more duplex nucleotides in length. Theinvention provides methods of inhibiting the expression of alignocellulosic enzyme, e.g., a cellulase or cellobiohydrolase, in acell comprising administering to the cell or expressing in the cell adouble-stranded inhibitory RNA (siRNA or miRNA), wherein the RNAcomprises a subsequence of a sequence of the invention.

In alternative embodiments the e invention provides isolated, syntheticor recombinant polypeptides comprising an amino acid sequence having atleast about 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%,62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%,76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%,90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or more, or complete(100%) sequence identity to an exemplary polypeptide or peptide of theinvention over a region of at least about 10, 15, 20, 25, 30, 35, 40,45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 125, 150, 175, 200,225, 250, 275, 300, 325, 350 or more residues, or over the full lengthof the polypeptide. In one aspect, the sequence identities aredetermined by analysis with a sequence comparison algorithm or by avisual inspection. Exemplary polypeptide or peptide sequences of theinvention include SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8,SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18,SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28,SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38,SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48,SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58,SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68,SEQ ID NO:70, SEQ ID NO:72, SEQ ID NO:74, SEQ ID NO:76, SEQ ID NO:78,SEQ ID NO:80, SEQ ID NO:82, SEQ ID NO:84, SEQ ID NO:86, SEQ ID NO:88,SEQ ID NO:90, SEQ ID NO:92, SEQ ID NO:94, SEQ ID NO:96, SEQ ID NO:98,SEQ ID NO:100, SEQ ID NO:102, SEQ ID NO:104, SEQ ID NO:106, SEQ IDNO:108, SEQ ID NO:110, SEQ ID NO:112, SEQ ID NO:114, SEQ ID NO:116, SEQID NO:118, SEQ ID NO:120, SEQ ID NO:122, SEQ ID NO:124, SEQ ID NO:126,SEQ ID NO:128, SEQ ID NO:130, SEQ ID NO:132, SEQ ID NO:134, and SEQ IDNO:136.

In alternative embodiments the lignocellulosic enzyme activity can bethermotolerant. The polypeptide can retain a lignocellulosic enzymeactivity after exposure to a temperature in the range from about −100°C. to about −80° C., about −80° C. to about −40° C., about −40° C. toabout −20° C., about −20° C. to about 0° C., about 0° C. to about 5° C.,about 5° C. to about 15° C., about 15° C. to about 25° C., about 25° C.to about 37° C., about 37° C. to about 45° C., about 45° C. to about 55°C., about 55° C. to about 70° C., about 70° C. to about 75° C., about75° C. to about 85° C., about 85° C. to about 90° C., about 90° C. toabout 95° C., about 95° C. to about 100° C., about 100° C. to about 105°C., about 105° C. to about 110° C., about 110° C. to about 120° C., or95° C., 96° C., 97° C., 98° C., 99° C., 100° C., 101° C., 102° C., 103°C., 104° C., 105° C., 106° C., 107° C., 108° C., 109° C., 110° C., 111°C., 112° C., 113° C., 114° C., 115° C. or more. In some embodiments, thethermotolerant polypeptides according to the invention retain alignocellulosic enzyme activity, after exposure to a temperature in theranges described above, at about pH 3.0, about pH 3.5, about pH 4.0,about pH 4.5, about pH 5.0, about pH 5.5, about pH 6.0, about pH 6.5,about pH 7.0, about pH 7.5, about pH 8.0, about pH 8.5, about pH 9.0,about pH 9.5, about pH 10.0, about pH 10.5, about pH 11.0, about pH11.5, about pH 12.0 or more.

In alternative embodiments the invention provides an isolated, syntheticor recombinant polypeptide or peptide comprising at least 10, 15, 20,25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 125,150 or more consecutive bases of a polypeptide or peptide sequence ofthe invention, sequences substantially identical thereto, and thesequences complementary thereto. The peptide can be, e.g., animmunogenic fragment, a motif (e.g., a binding site), a signal sequence,a prepro sequence or an active site.

In alternative embodiments the invention provides isolated, synthetic orrecombinant nucleic acids comprising a sequence encoding a polypeptidehaving a lignocellulosic activity, e.g., a cellulose and/or acellobiohydrolase activity, and a signal sequence, wherein the nucleicacid comprises a sequence of the invention. The signal sequence can bederived from another the lignocellulosic enzyme, e.g., a heterologousenzyme. The invention provides isolated, synthetic or recombinantnucleic acids comprising a sequence encoding a polypeptide having alignocellulosic activity, e.g., a cellulose and/or a cellobiohydrolaseactivity, wherein the sequence does not contain a signal sequence andthe nucleic acid comprises a sequence of the invention. In one aspect,the invention provides an isolated, synthetic or recombinant polypeptidecomprising a polypeptide of the invention lacking all or part of asignal sequence. In one aspect, the isolated, synthetic or recombinantpolypeptide can comprise the polypeptide of the invention comprising aheterologous signal sequence, such as a heterologous the lignocellulosicenzyme signal sequence.

In alternative embodiments the invention provides chimeric (e.g.,multidomain recombinant) proteins comprising a first domain comprising asignal sequence and/or a carbohydrate binding domain (CBM) and at leasta second domain. The protein can be a fusion protein. The second domaincan comprise an enzyme. The chimeric protein can comprise a signalsequence and/or a CBM and a structural protein.

In alternative embodiments the invention provides chimeric polypeptidescomprising (i) at least a first domain comprising (or consisting of) acarbohydrate binding domain (CBM), a signal peptide (SP), a preprosequence and/or a catalytic domain (CD) of the invention; and, (ii) atleast a second domain comprising a heterologous polypeptide or peptide,wherein the heterologous polypeptide or peptide is not naturallyassociated with the CBM, signal peptide (SP), prepro sequence and/orcatalytic domain (CD). In one aspect, the heterologous polypeptide orpeptide is not a lignocellulosic enzyme. The heterologous polypeptide orpeptide can be amino terminal to, carboxy terminal to or on both ends ofthe CBM, signal peptide (SP), prepro sequence and/or catalytic domain(CD).

In alternative embodiments the invention provides isolated, synthetic orrecombinant nucleic acids encoding a chimeric polypeptide, wherein thechimeric polypeptide comprises at least a first domain comprising, orconsisting of, a CBM, a signal peptide (SP), a prepro domain and/or acatalytic domain (CD) of the invention; and, at least a second domaincomprising a heterologous polypeptide or peptide, wherein theheterologous polypeptide or peptide is not naturally associated with theCBM, signal peptide (SP), prepro domain and/or catalytic domain (CD).

In alternative embodiments the invention provides isolated, synthetic orrecombinant signal sequences (e.g., signal peptides) consisting of orcomprising the sequence of (a sequence as set forth in) residues 1 to14, 1 to 15, 1 to 16, 1 to 17, 1 to 18, 1 to 19, 1 to 20, 1 to 21, 1 to22, 1 to 23, 1 to 24, 1 to 25, 1 to 26, 1 to 27, 1 to 28, 1 to 28, 1 to30, 1 to 31, 1 to 32, 1 to 33, 1 to 34, 1 to 35, 1 to 36, 1 to 37, 1 to38, 1 to 40, 1 to 41, 1 to 42, 1 to 43, 1 to 44, 1 to 45, 1 to 46 or 1to 47, of a polypeptide of the invention, e.g., the exemplarypolypeptides of the invention.

In alternative embodiments the lignocellulosic enzyme, e.g., cellulaseor cellobiohydrolase, activity comprises a specific activity at about37° C. in the range from about 1 to about 1200 units per milligram ofprotein, or, about 100 to about 1000 units per milligram of protein. Inanother aspect, the lignocellulosic enzyme activity comprises a specificactivity from about 100 to about 1000 units per milligram of protein,or, from about 500 to about 750 units per milligram of protein.Alternatively, the lignocellulosic enzyme activity comprises a specificactivity at 37° C. in the range from about 1 to about 750 units permilligram of protein, or, from about 500 to about 1200 units permilligram of protein. In one aspect, the lignocellulosic enzyme activitycomprises a specific activity at 37° C. in the range from about 1 toabout 500 units per milligram of protein, or, from about 750 to about1000 units per milligram of protein. In another aspect, thelignocellulosic enzyme activity comprises a specific activity at 37° C.in the range from about 1 to about 250 units per milligram of protein.Alternatively, the lignocellulosic enzyme activity comprises a specificactivity at 37° C. in the range from about 1 to about 100 units permilligram of protein.

In alternative embodiments the thermotolerance comprises retention of atleast half of the specific activity of the lignocellulosic enzyme at 37°C. after being heated to the elevated temperature. Alternatively, thethermotolerance can comprise retention of specific activity at 37° C. inthe range from about 1 to about 1200 units per milligram of protein, or,from about 500 to about 1000 units per milligram of protein, after beingheated to the elevated temperature. In another aspect, thethermotolerance can comprise retention of specific activity at 37° C. inthe range from about 1 to about 500 units per milligram of protein afterbeing heated to the elevated temperature.

In alternative embodiments, isolated, synthetic or recombinantpolypeptides of the invention comprise at least one glycosylation site.In one aspect, glycosylation can be an N-linked glycosylation. In oneaspect, the polypeptide can be glycosylated after being expressed in anAspergillus, e.g., an Aspergillus niger, a Pichia, e.g., a Pichiapastoris, a Schizosaccharomyces, e.g., a Schizosaccharomyces pombe,and/or a Pseudomonas, e.g., a Pseudomonas fluorescens. In alternativeembodiments, nucleic acids of the invention are expressed in anAspergillus, e.g., an Aspergillus niger, a Pichia, e.g., a Pichiapastoris, a Schizosaccharomyces, e.g., a Schizosaccharomyces pombe,and/or a Pseudomonas, e.g., a Pseudomonas fluorescens; e.g., to expresspolypeptides of the invention.

In alternative embodiments the polypeptide can retain the activity underconditions comprising about pH 6.5, pH 6, pH 5.5, pH 5, pH 4.5 or pH 4or more acidic. In another aspect, the polypeptide can retain thelignocellulosic enzyme activity under conditions comprising about pH 7,pH 7.5 pH 8.0, pH 8.5, pH 9, pH 9.5, pH 10, pH 10.5 or pH 11 or morebasic pH. In one aspect, the polypeptide can retain the lignocellulosicenzyme activity after exposure to conditions comprising about pH 6.5, pH6, pH 5.5, pH 5, pH 4.5 or pH 4 or more acidic pH. In another aspect,the polypeptide can retain the lignocellulosic enzyme activity afterexposure to conditions comprising about pH 7, pH 7.5 pH 8.0, pH 8.5, pH9, pH 9.5, pH 10, pH 10.5 or pH 11 or more basic pH.

In alternative embodiments the lignocellulosic enzyme has activity atunder alkaline conditions, e.g., the alkaline conditions of the gut,e.g., the small intestine. In one aspect, the polypeptide can retainsactivity after exposure to the acidic pH of the stomach.

In alternative embodiments the invention provides protein preparationscomprising a polypeptide (including peptides) of the invention, whereinthe protein preparation comprises a liquid, a solid or a gel. Theinvention provides heterodimers comprising a polypeptide of theinvention and a second protein or domain. The second member of theheterodimer can be a different lignocellulosic enzyme or anotherprotein. In one aspect, the second domain can be a polypeptide and theheterodimer can be a fusion protein. In one aspect, the second domaincan be an epitope or a tag. In one aspect, the invention provideshomodimers comprising a polypeptide of the invention.

In alternative embodiments the invention provides immobilizedpolypeptides (including peptides) comprising or consisting ofpolypeptides of the invention, a polypeptide encoded by a nucleic acidof the invention, or a polypeptide comprising a polypeptide of theinvention and a second domain. In one aspect, the polypeptide can beimmobilized on a cell, a metal, a resin, a polymer, a ceramic, a glass,a microelectrode, a graphitic particle, a bead, a gel, a plate, an arrayor a capillary tube. The invention also provides arrays comprisingpolypeptides of the invention, or an immobilized nucleic acid of theinvention, including, e.g., probes of the invention. The invention alsoprovides arrays comprising an antibody of the invention.

In alternative embodiments the invention provides isolated, synthetic orrecombinant antibodies that specifically bind to a polypeptide of theinvention or to a polypeptide encoded by a nucleic acid of theinvention. These antibodies of the invention can be a monoclonal or apolyclonal antibody. The invention provides hybridomas comprising anantibody of the invention, e.g., an antibody that specifically binds toa polypeptide of the invention or to a polypeptide encoded by a nucleicacid of the invention. The invention provides nucleic acids encodingthese antibodies.

The invention provides method of isolating or identifying a polypeptidehaving a lignocellulosic enzyme activity, e.g., cellulase orcellobiohydrolase activity, comprising the steps of: (a) providing anantibody of the invention; (b) providing a sample comprisingpolypeptides; and (c) contacting the sample of step (b) with theantibody of step (a) under conditions wherein the antibody canspecifically bind to the polypeptide, thereby isolating or identifying apolypeptide having the lignocellulosic enzyme activity.

In alternative embodiments the invention provides methods of making ananti-cellulase, e.g., anti-cellobiohydrolase, enzyme antibody comprisingadministering to a non-human animal a nucleic acid of the invention or apolypeptide of the invention or subsequences thereof in an amountsufficient to generate a humoral immune response, thereby making theanti-enzyme antibody. The invention provides methods of making ananti-enzyme immune response(s) (cellular or humoral) comprisingadministering to a non-human animal a nucleic acid of the invention or apolypeptide of the invention or subsequences thereof in an amountsufficient to generate an immune response (cellular or humoral).

In alternative embodiments the invention provides methods of producing arecombinant polypeptide comprising the steps of: (a) providing a nucleicacid of the invention operably linked to a promoter; and (b) expressingthe nucleic acid of step (a) under conditions that allow expression ofthe polypeptide, thereby producing a recombinant polypeptide. In oneaspect, the method can further comprise transforming a host cell withthe nucleic acid of step (a) followed by expressing the nucleic acid ofstep (a), thereby producing a recombinant polypeptide in a transformedcell.

In alternative embodiments the invention provides methods foridentifying a polypeptide having a lignocellulosic enzyme activity,e.g., cellulase or cellobiohydrolase enzyme activity, comprising thefollowing steps: (a) providing a polypeptide of the invention; or apolypeptide encoded by a nucleic acid of the invention; (b) providingthe lignocellulosic enzyme substrate; and (c) contacting the polypeptideor a fragment or variant thereof of step (a) with the substrate of step(b) and detecting a decrease in the amount of substrate or an increasein the amount of a reaction product, wherein a decrease in the amount ofthe substrate or an increase in the amount of the reaction productdetects a polypeptide having the lignocellulosic enzyme activity. In oneaspect, the substrate is a cellulose-comprising or apolysaccharide-comprising (e.g., soluble cellooligsaccharide- and/orarabinoxylan oligomer-comprising) compound.

In alternative embodiments the invention provides methods foridentifying a lignocellulosic enzyme, e.g., a cellulase orcellobiohydrolase, substrate comprising the following steps: (a)providing a polypeptide of the invention; or a polypeptide encoded by anucleic acid of the invention; (b) providing a test substrate; and (c)contacting the polypeptide of step (a) with the test substrate of step(b) and detecting a decrease in the amount of substrate or an increasein the amount of reaction product, wherein a decrease in the amount ofthe substrate or an increase in the amount of a reaction productidentifies the test substrate as a lignocellulosic enzyme substrate.

In alternative embodiments the invention provides methods of determiningwhether a test compound specifically binds to a polypeptide comprisingthe following steps: (a) expressing a nucleic acid or a vectorcomprising the nucleic acid under conditions permissive for translationof the nucleic acid to a polypeptide, wherein the nucleic acid comprisesa nucleic acid of the invention, or, providing a polypeptide of theinvention; (b) providing a test compound; (c) contacting the polypeptidewith the test compound; and (d) determining whether the test compound ofstep (b) specifically binds to the polypeptide.

In alternative embodiments the invention provides methods foridentifying a modulator of a lignocellulosic enzyme comprising thefollowing steps: (a) providing a polypeptide of the invention or apolypeptide encoded by a nucleic acid of the invention; (b) providing atest compound; (c) contacting the polypeptide of step (a) with the testcompound of step (b) and measuring an activity of the lignocellulosicenzyme, wherein a change in the lignocellulosic enzyme activity measuredin the presence of the test compound compared to the activity in theabsence of the test compound provides a determination that the testcompound modulates the lignocellulosic enzyme activity. In one aspect,the lignocellulosic enzyme activity can be measured by providing alignocellulosic enzyme substrate and detecting a decrease in the amountof the substrate or an increase in the amount of a reaction product, or,an increase in the amount of the substrate or a decrease in the amountof a reaction product. A decrease in the amount of the substrate or anincrease in the amount of the reaction product with the test compound ascompared to the amount of substrate or reaction product without the testcompound identifies the test compound as an activator of thelignocellulosic enzyme activity. In alternative embodiments an increasein the amount of the substrate or a decrease in the amount of thereaction product with the test compound as compared to the amount ofsubstrate or reaction product without the test compound identifies thetest compound as an inhibitor of the lignocellulosic enzyme activity.

In alternative embodiments the invention provides computer systemscomprising a processor and a data storage device wherein said datastorage device has stored thereon a polypeptide sequence or a nucleicacid sequence of the invention (e.g., a polypeptide or peptide encodedby a nucleic acid of the invention). In one aspect, the computer systemcan further comprise a sequence comparison algorithm and a data storagedevice having at least one reference sequence stored thereon. In anotheraspect, the sequence comparison algorithm comprises a computer programthat indicates polymorphisms. In one aspect, the computer system canfurther comprise an identifier that identifies one or more features insaid sequence. The invention provides computer readable media havingstored thereon a polypeptide sequence or a nucleic acid sequence of theinvention. The invention provides methods for identifying a feature in asequence comprising the steps of: (a) reading the sequence using acomputer program which identifies one or more features in a sequence,wherein the sequence comprises a polypeptide sequence or a nucleic acidsequence of the invention; and (b) identifying one or more features inthe sequence with the computer program. The invention provides methodsfor comparing a first sequence to a second sequence comprising the stepsof: (a) reading the first sequence and the second sequence through useof a computer program which compares sequences, wherein the firstsequence comprises a polypeptide sequence or a nucleic acid sequence ofthe invention; and (b) determining differences between the firstsequence and the second sequence with the computer program. The step ofdetermining differences between the first sequence and the secondsequence can further comprise the step of identifying polymorphisms. Inone aspect, the method can further comprise an identifier thatidentifies one or more features in a sequence. In another aspect, themethod can comprise reading the first sequence using a computer programand identifying one or more features in the sequence.

In alternative embodiments the invention provides methods for isolatingor recovering a nucleic acid encoding a polypeptide having thelignocellulosic enzyme, e.g., cellulase or cellobiohydrolase, from asample, e.g. an environmental sample, comprising the steps of: (a)providing an amplification primer sequence pair for amplifying a nucleicacid encoding a polypeptide having a lignocellulosic activity, whereinthe primer pair is capable of amplifying a nucleic acid of theinvention; (b) isolating a nucleic acid from the sample, e.g.environmental sample, or treating the sample, e.g. environmental sample,such that nucleic acid in the sample is accessible for hybridization tothe amplification primer pair; and, (c) combining the nucleic acid ofstep (b) with the amplification primer pair of step (a) and amplifyingnucleic acid from the sample, e.g. environmental sample, therebyisolating or recovering a nucleic acid encoding a polypeptide having alignocellulosic activity from a sample, e.g. an environmental sample.One or each member of the amplification primer sequence pair cancomprise an oligonucleotide comprising an amplification primer sequencepair of the invention, e.g., having at least about 10 to 50 consecutivebases of a sequence of the invention.

In alternative embodiments the invention provides methods for isolatingor recovering a nucleic acid encoding a polypeptide having alignocellulosic activity, e.g., cellulase or cellobiohydrolase activity,from a sample, e.g. an environmental sample, comprising the steps of:(a) providing a polynucleotide probe comprising a nucleic acid of theinvention or a subsequence thereof; (b) isolating a nucleic acid fromthe sample, e.g. environmental sample, or treating the sample, e.g.environmental sample, such that nucleic acid in the sample is accessiblefor hybridization to a polynucleotide probe of step (a); (c) combiningthe isolated nucleic acid or the treated sample, e.g. environmentalsample, of step (b) with the polynucleotide probe of step (a); and (d)isolating a nucleic acid that specifically hybridizes with thepolynucleotide probe of step (a), thereby isolating or recovering anucleic acid encoding a polypeptide having a lignocellulosic activityfrom a sample, e.g. an environmental sample. The sample, e.g.environmental sample, can comprise a water sample, a liquid sample, asoil sample, an air sample or a biological sample. In one aspect, thebiological sample can be derived from a bacterial cell, a protozoancell, an insect cell, a yeast cell, a plant cell, a fungal cell or amammalian cell.

In alternative embodiments the invention provides methods of generatinga variant of a nucleic acid encoding a polypeptide having alignocellulosic activity, e.g., cellulase or cellobiohydrolase activity,comprising the steps of: (a) providing a template nucleic acidcomprising a nucleic acid of the invention; and (b) modifying, deletingor adding one or more nucleotides in the template sequence, or acombination thereof, to generate a variant of the template nucleic acid.In one aspect, the method can further comprise expressing the variantnucleic acid to generate a variant the lignocellulosic enzymepolypeptide. The modifications, additions or deletions can be introducedby a method comprising error-prone PCR, shuffling,oligonucleotide-directed mutagenesis, assembly PCR, sexual PCRmutagenesis, in vivo mutagenesis, cassette mutagenesis, recursiveensemble mutagenesis, exponential ensemble mutagenesis, site-specificmutagenesis, GeneReassembly, Gene Site Saturation Mutagensis (or GSSM),Tailored Multi-Site Combinatorial Assembly, Chromosomal SaturationMutagenesis (CSM) or a combination thereof. In another aspect, themodifications, additions or deletions are introduced by a methodcomprising recombination, recursive sequence recombination,phosphothioate-modified DNA mutagenesis, uracil-containing templatemutagenesis, gapped duplex mutagenesis, point mismatch repairmutagenesis, repair-deficient host strain mutagenesis, chemicalmutagenesis, radiogenic mutagenesis, deletion mutagenesis,restriction-selection mutagenesis, restriction-purification mutagenesis,artificial gene synthesis, ensemble mutagenesis, chimeric nucleic acidmultimer creation and a combination thereof.

In alternative embodiments the method can be iteratively repeated untila lignocellulosic enzyme, e.g., a cellobiohydrolase enzyme having analtered or different activity or an altered or different stability fromthat of a polypeptide encoded by the template nucleic acid is produced.In one aspect, the variant the lignocellulosic enzyme polypeptide isthermotolerant, and retains some activity after being exposed to anelevated temperature. In another aspect, the variant the lignocellulosicenzyme polypeptide has increased glycosylation as compared to thelignocellulosic enzyme encoded by a template nucleic acid.Alternatively, the variant the polypeptide has a lignocellulosic enzymeactivity under a high temperature, wherein the lignocellulosic enzymeencoded by the template nucleic acid is not active under the hightemperature. In one aspect, the method can be iteratively repeated untila lignocellulosic enzyme coding sequence having an altered codon usagefrom that of the template nucleic acid is produced. In another aspect,the method can be iteratively repeated until a lignocellulosic enzymegene having higher or lower level of message expression or stabilityfrom that of the template nucleic acid is produced.

In alternative embodiments the invention provides methods for modifyingcodons in a nucleic acid encoding a polypeptide having a lignocellulosicactivity to increase its expression in a host cell, the methodcomprising the following steps: (a) providing a nucleic acid of theinvention encoding a polypeptide having a lignocellulosic enzymeactivity; and, (b) identifying a non-preferred or a less preferred codonin the nucleic acid of step (a) and replacing it with a preferred orneutrally used codon encoding the same amino acid as the replaced codon,wherein a preferred codon is a codon over-represented in codingsequences in genes in the host cell and a non-preferred or lesspreferred codon is a codon under-represented in coding sequences ingenes in the host cell, thereby modifying the nucleic acid to increaseits expression in a host cell.

In alternative embodiments the invention provides methods for modifyingcodons in a nucleic acid encoding a polypeptide having a lignocellulosicactivity; the method comprising the following steps: (a) providing anucleic acid of the invention; and, (b) identifying a codon in thenucleic acid of step (a) and replacing it with a different codonencoding the same amino acid as the replaced codon, thereby modifyingcodons in a nucleic acid encoding a lignocellulosic enzyme.

In alternative embodiments the invention provides methods for modifyingcodons in a nucleic acid encoding a polypeptide having a lignocellulosicactivity to increase its expression in a host cell, the methodcomprising the following steps: (a) providing a nucleic acid of theinvention encoding a lignocellulosic enzyme polypeptide; and, (b)identifying a non-preferred or a less preferred codon in the nucleicacid of step (a) and replacing it with a preferred or neutrally usedcodon encoding the same amino acid as the replaced codon, wherein apreferred codon is a codon over-represented in coding sequences in genesin the host cell and a non-preferred or less preferred codon is a codonunder-represented in coding sequences in genes in the host cell, therebymodifying the nucleic acid to increase its expression in a host cell. Inalternative embodiments the invention provides methods for modifying acodon in a nucleic acid encoding a polypeptide having a lignocellulosicactivity to decrease its expression in a host cell, the methodcomprising the following steps: (a) providing a nucleic acid of theinvention; and (b) identifying at least one preferred codon in thenucleic acid of step (a) and replacing it with a non-preferred or lesspreferred codon encoding the same amino acid as the replaced codon,wherein a preferred codon is a codon over-represented in codingsequences in genes in a host cell and a non-preferred or less preferredcodon is a codon under-represented in coding sequences in genes in thehost cell, thereby modifying the nucleic acid to decrease its expressionin a host cell. In one aspect, the host cell can be a bacterial cell, afungal cell, an insect cell, a yeast cell, a plant cell or a mammaliancell. In alternative embodiments, host cells are bacterial cellsincluding any species within the genera Aspergillus, Escherichia,Bacillus, Streptomyces, Salmonella, Pseudomonas, Lactococcus, andStaphylococcus, including, e.g., Escherichia coli, Lactococcus lactis,Bacillus subtilis, Bacillus cereus, Salmonella typhimurium, Pseudomonasfluorescens. In alternative embodiments, host cells are fungal cellsincluding any species of Aspergillus, including Aspergillus niger. Inalternative embodiments, host cells are yeast cells including anyspecies of an Aspergillus, Pichia, Saccharomyces, Schizosaccharomyces,or Schwanniomyces, including Aspergillus niger, Pichia pastoris,Saccharomyces cerevisiae, or Schizosaccharomyces pombe.

In alternative embodiments the invention provides methods for producinga library of nucleic acids encoding a plurality of modifiedlignocellulosic enzyme, e.g., cellulase or cellobiohydrolase, activesites or substrate binding sites, wherein the modified active sites orsubstrate binding sites are derived from a first nucleic acid comprisinga sequence encoding a first active site or a first substrate bindingsite the method comprising the following steps: (a) providing a firstnucleic acid encoding a first active site or first substrate bindingsite, wherein the first nucleic acid sequence comprises a sequence thathybridizes under stringent conditions to a nucleic acid of theinvention, and the nucleic acid encodes a lignocellulosic enzyme activesite or a lignocellulosic enzyme substrate binding site; (b) providing aset of mutagenic oligonucleotides that encode naturally-occurring aminoacid variants at a plurality of targeted codons in the first nucleicacid; and, (c) using the set of mutagenic oligonucleotides to generate aset of active site-encoding or substrate binding site-encoding variantnucleic acids encoding a range of amino acid variations at each aminoacid codon that was mutagenized, thereby producing a library of nucleicacids encoding a plurality of modified the lignocellulosic enzyme activesites or substrate binding sites. In one aspect, the method comprisesmutagenizing the first nucleic acid of step (a) by a method comprisingan optimized directed evolution system, Gene Site SaturationMutagenesis^(SM) (or GSSM^(SM)) technology, GeneReassembly^(SM)technology, Tailored Multi-Site Combinatorial Assembly^(SM) technology,error-prone PCR, shuffling, oligonucleotide-directed mutagenesis,assembly PCR, sexual PCR mutagenesis, in vivo mutagenesis, cassettemutagenesis, recursive ensemble mutagenesis, exponential ensemblemutagenesis, site-specific mutagenesis, and a combination thereof. Inanother aspect, the method comprises mutagenizing the first nucleic acidof step (a) or variants by a method comprising recombination, recursivesequence recombination, phosphothioate-modified DNA mutagenesis,uracil-containing template mutagenesis, gapped duplex mutagenesis, pointmismatch repair mutagenesis, repair-deficient host strain mutagenesis,chemical mutagenesis, radiogenic mutagenesis, deletion mutagenesis,restriction-selection mutagenesis, restriction-purification mutagenesis,artificial gene synthesis, ensemble mutagenesis, chimeric nucleic acidmultimer creation and a combination thereof.

In alternative embodiments the invention provides methods for making asmall molecule comprising the following steps: (a) providing a pluralityof biosynthetic enzymes capable of synthesizing or modifying a smallmolecule, wherein one of the enzymes comprises a lignocellulosic enzyme,e.g., a cellulase or cellobiohydrolase, encoded by a nucleic acid of theinvention; (b) providing a substrate for at least one of the enzymes ofstep (a); and (c) reacting the substrate of step (b) with the enzymesunder conditions that facilitate a plurality of biocatalytic reactionsto generate a small molecule by a series of biocatalytic reactions. Theinvention provides methods for modifying a small molecule comprising thefollowing steps: (a) providing a lignocellulosic enzyme, wherein theenzyme comprises a polypeptide of the invention, or, a polypeptideencoded by a nucleic acid of the invention, or a subsequence thereof;(b) providing a small molecule; and (c) reacting the enzyme of step (a)with the small molecule of step (b) under conditions that facilitate anenzymatic reaction catalyzed by the lignocellulosic enzyme, therebymodifying a small molecule by a lignocellulosic enzymatic reaction. Inone aspect, the method can comprise a plurality of small moleculesubstrates for the enzyme of step (a), thereby generating a library ofmodified small molecules produced by at least one enzymatic reactioncatalyzed by the lignocellulosic enzyme. In one aspect, the method cancomprise a plurality of additional enzymes under conditions thatfacilitate a plurality of biocatalytic reactions by the enzymes to forma library of modified small molecules produced by the plurality ofenzymatic reactions. In another aspect, the method can further comprisethe step of testing the library to determine if a particular modifiedsmall molecule that exhibits a desired activity is present within thelibrary. The step of testing the library can further comprise the stepsof systematically eliminating all but one of the biocatalytic reactionsused to produce a portion of the plurality of the modified smallmolecules within the library by testing the portion of the modifiedsmall molecule for the presence or absence of the particular modifiedsmall molecule with a desired activity, and identifying at least onespecific biocatalytic reaction that produces the particular modifiedsmall molecule of desired activity.

In alternative embodiments the invention provides methods fordetermining a functional fragment of an enzyme of the inventioncomprising the steps of: (a) providing a polypeptide of the invention,or a polypeptide encoded by a nucleic acid of the invention, or asubsequence thereof; and (b) deleting a plurality of amino acid residuesfrom the sequence of step (a) and testing the remaining subsequence forlignocellulosic enzyme activity, thereby determining a functionalfragment of the enzyme. In one aspect, lignocellulosic enzyme activity,is measured by providing a substrate and detecting a decrease in theamount of the substrate or an increase in the amount of a reactionproduct.

In alternative embodiments the invention provides methods of increasingthermotolerance or thermostability of a lignocellulosic enzyme, themethod comprising glycosylating a lignocellulosic enzyme polypeptide,wherein the polypeptide comprises at least thirty contiguous amino acidsof a polypeptide of the invention; or a polypeptide encoded by a nucleicacid sequence of the invention, thereby increasing the thermotoleranceor thermostability of the lignocellulosic enzyme polypeptide. In oneaspect, the lignocellulosic enzyme specific activity can be thermostableor thermotolerant at a temperature in the range from greater than about37° C. to about 95° C.

In alternative embodiments the invention provides methods foroverexpressing a recombinant glucose oxidase and/or the lignocellulosicenzyme polypeptide in a cell comprising expressing a vector comprising anucleic acid comprising a nucleic acid of the invention or a nucleicacid sequence of the invention, wherein the sequence identities aredetermined by analysis with a sequence comparison algorithm or by visualinspection, wherein overexpression is effected by use of a high activitypromoter, a dicistronic vector or by gene amplification of the vector.

In alternative embodiments the invention provides methods of making atransgenic plant comprising the following steps: (a) introducing aheterologous nucleic acid sequence into the cell, wherein theheterologous nucleic sequence comprises a nucleic acid sequence of theinvention, thereby producing a transformed plant cell; and (b) producinga transgenic plant from the transformed cell. In one aspect, the step(a) can further comprise introducing the heterologous nucleic acidsequence by electroporation or microinjection of plant cell protoplasts.In another aspect, the step (a) can further comprise introducing theheterologous nucleic acid sequence directly to plant tissue by DNAparticle bombardment. Alternatively, the step (a) can further compriseintroducing the heterologous nucleic acid sequence into the plant cellDNA using an Agrobacterium tumefaciens host. In one aspect, the plantcell can be a cane sugar, beet, soybean, tomato, potato, corn, rice,wheat, tobacco or barley cell. The cell can be derived from a monocot ora dicot, or a monocot corn, sugarcane, rice, wheat, barley, switchgrassor Miscanthus; or a dicot oilseed crop, soy, canola, rapeseed, flax,cotton, palm oil, sugar beet, peanut, tree, poplar or lupine.

In alternative embodiments the invention provides methods of expressinga heterologous nucleic acid sequence in a plant cell comprising thefollowing steps: (a) transforming the plant cell with a heterologousnucleic acid sequence operably linked to a promoter, wherein theheterologous nucleic sequence comprises a nucleic acid of the invention;(b) growing the plant under conditions wherein the heterologous nucleicacids sequence is expressed in the plant cell. The invention providesmethods of expressing a heterologous nucleic acid sequence in a plantcell comprising the following steps: (a) transforming the plant cellwith a heterologous nucleic acid sequence operably linked to a promoter,wherein the heterologous nucleic sequence comprises a sequence of theinvention; (b) growing the plant under conditions wherein theheterologous nucleic acids sequence is expressed in the plant cell. Inone aspect, the promoter is or comprises: a viral, bacterial, mammalianor plant promoter; or, a plant promoter; or, a potato, rice, corn,wheat, tobacco or barley promoter; or, a constitutive promoter or aCaMV35S promoter; or, an inducible promoter; or, a tissue-specificpromoter or an environmentally regulated or a developmentally regulatedpromoter; or, a seed-specific, a leaf-specific, a root-specific, astem-specific or an abscission-induced promoter; or, a seed preferredpromoter, a maize gamma zein promoter or a maize ADP-gpp promoter. Inone aspect, the plant cell is derived from is a monocot or dicot, or theplant is a monocot corn, sugarcane, rice, wheat, barley, switchgrass orMiscanthus; or the plant is a dicot oilseed crop, soy, canola, rapeseed,flax, cotton, palm oil, sugar beet, peanut, tree, poplar or lupine.

In alternative embodiments the invention provides methods forhydrolyzing, breaking up or disrupting a cellooligsaccharide, anarabinoxylan oligomer, or a glucan- or cellulose-comprising compositioncomprising the following steps: (a) providing a polypeptide of theinvention; (b) providing a composition comprising a cellulose or aglucan; and (c) contacting the polypeptide of step (a) with thecomposition of step (b) under conditions wherein the cellulasehydrolyzes, breaks up or disrupts the cellooligsaccharide, arabinoxylanoligomer, or glucan- or cellulose-comprising composition; whereinoptionally the composition comprises a plant cell, a bacterial cell, ayeast cell, an insect cell, or an animal cell. In one aspect, thepolypeptide of the invention has a lignocellulosic activity, e.g., anactivity comprising a cellulase or cellobiohydrolase activity.

In alternative embodiments the invention provides feeds or foodscomprising a polypeptide of the invention, or a polypeptide encoded by anucleic acid of the invention. In one aspect, the invention provides afood, feed, a liquid, e.g., a beverage (such as a fruit juice or abeer), a bread or a dough or a bread product, or a beverage precursor(e.g., a wort), comprising a polypeptide of the invention. The inventionprovides food or nutritional supplements for an animal comprising apolypeptide of the invention, e.g., a polypeptide encoded by the nucleicacid of the invention. In one aspect, the polypeptide of the inventionhas a lignocellulosic activity, e.g., an activity comprising a cellulaseor cellobiohydrolase activity.

In alternative embodiments the polypeptide in the food or nutritionalsupplement can be glycosylated. The invention provides edible enzymedelivery matrices comprising a polypeptide of the invention, e.g., apolypeptide encoded by the nucleic acid of the invention. In one aspect,the delivery matrix comprises a pellet. In one aspect, the polypeptidecan be glycosylated. In one aspect, the lignocellulosic enzyme, e.g.,cellulase or cellobiohydrolase activity is thermotolerant. In anotheraspect, the lignocellulosic enzyme activity is thermostable.

In alternative embodiments the invention provides a food, a feed or anutritional supplement comprising a polypeptide of the invention. Theinvention provides methods for utilizing a lignocellulosic enzyme of theinvention, e.g., cellulase or cellobiohydrolase, as a nutritionalsupplement in an animal or human diet, the method comprising: preparinga nutritional supplement containing a lignocellulosic enzyme of theinvention comprising at least thirty contiguous amino acids of apolypeptide of the invention; and administering the nutritionalsupplement to an animal. The animal can be a human, a ruminant or amonogastric animal. The lignocellulosic enzyme can be prepared byexpression of a polynucleotide encoding the lignocellulosic enzyme in ahost organism, e.g., a bacterium, a yeast, a plant, an insect, a fungusand/or an animal. The organism also can be an S. pombe, S. cerevisiae,Pichia pastoris, E. coli, Streptomyces sp., Bacillus sp. and/orLactobacillus sp. In one aspect, the plant is a monocot or dicot, or theplant is a monocot corn, sugarcane, rice, wheat, barley, switchgrass orMiscanthus; or the plant is a dicot oilseed crop, soy, canola, rapeseed,flax, cotton, palm oil, sugar beet, peanut, tree, poplar or lupine.

In alternative embodiments the invention provides edible enzyme deliverymatrix comprising a thermostable recombinant of a lignocellulosic enzymeof the invention, e.g., cellulase or cellobiohydrolase of the invention.The invention provides methods for delivering a lignocellulosic enzymesupplement to an animal or human, the method comprising: preparing anedible enzyme delivery matrix in the form of pellets comprising agranulate edible carrier and a thermostable recombinant thelignocellulosic enzyme, wherein the pellets readily disperse thelignocellulosic enzyme contained therein into aqueous media, andadministering the edible enzyme delivery matrix to the animal. Therecombinant lignocellulosic enzyme of the invention can comprise all ora subsequence of at least one polypeptide of the invention. Thelignocellulosic enzyme can be glycosylated to provide thermostability atpelletizing conditions. The delivery matrix can be formed by pelletizinga mixture comprising a grain germ and a lignocellulosic enzyme. Thepelletizing conditions can include application of steam. The pelletizingconditions can comprise application of a temperature in excess of about80° C. for about 5 minutes and the enzyme retains a specific activity ofat least 350 to about 900 units per milligram of enzyme.

In alternative embodiments the invention provides a pharmaceuticalcomposition comprising a lignocellulosic enzyme of the invention, or apolypeptide encoded by a nucleic acid of the invention. In one aspect,the pharmaceutical composition acts as a digestive aid.

In alternative embodiments a cellulose-containing compound is contactedto (reacted with) a polypeptide of the invention having alignocellulosic enzyme of the invention at a pH in the range of betweenabout pH 3.0 to 9.0, 10.0, 11.0 or more. In other aspects, acellulose-containing compound is contacted with the lignocellulosicenzyme at a temperature of about 55° C., 60° C., 65° C., 70° C., 75° C.,80° C., 85° C., 90° C., or more.

In alternative embodiments the invention provides methods for deliveringan enzyme supplement, e.g., comprising an enzyme of the invention, to ananimal or human, the method comprising: preparing an edible enzymedelivery matrix or pellets comprising a granulate edible carrier and athermostable recombinant enzyme of the invention, wherein the pelletsreadily disperse the cellulase enzyme contained therein into aqueousmedia, and the recombinant enzyme of the invention, or a polypeptideencoded by a nucleic acid of the invention; and, administering theedible enzyme delivery matrix or pellet to the animal; and optionallythe granulate edible carrier comprises a carrier selected from the groupconsisting of a grain germ, a grain germ that is spent of oil, a hay, analfalfa, a timothy, a soy hull, a sunflower seed meal and a wheat midd,and optionally the edible carrier comprises grain germ that is spent ofoil, and optionally the enzyme of the invention is glycosylated toprovide thermostability at pelletizing conditions, and optionally thedelivery matrix is formed by pelletizing a mixture comprising a graingerm and a cellulase, and optionally the pelletizing conditions includeapplication of steam, and optionally the pelletizing conditions compriseapplication of a temperature in excess of about 80° C. for about 5minutes and the enzyme retains a specific activity of at least 350 toabout 900 units per milligram of enzyme.

In alternative embodiments the invention provides cellulose- orcellulose derivative-compositions comprising a polypeptide of theinvention, or a polypeptide encoded by a nucleic acid of the invention,wherein in alternative embodiments the polypeptide has a cellulase orcellobiohydrolase activity.

In alternative embodiments the invention provides wood, wood pulp orwood products, or wood waste, comprising an enzyme of the invention, oran enzyme encoded by a nucleic acid of the invention, wherein optionallythe activity of the enzyme of the invention comprises cellulase orcellobiohydrolase activity.

In alternative embodiments the invention provides paper, paper pulp orpaper products, or paper waste byproducts or recycled material,comprising a polypeptide of the invention, or a polypeptide encoded by anucleic acid of the invention, wherein optionally the polypeptide hascellulase or cellobiohydrolase activity.

In alternative embodiments the invention provides methods for reducingthe amount of cellulose in a paper, a wood or wood product comprisingcontacting the paper, wood or wood product, or wood waste, with anenzyme of the invention, or an enzyme encoded by a nucleic acid of theinvention, wherein optionally the enzyme activity comprises a cellulaseor cellobiohydrolase activity.

In alternative embodiments the invention provides detergent compositionscomprising an enzyme of the invention, or an enzyme encoded by a nucleicacid of the invention, wherein optionally the polypeptide is formulatedin a non-aqueous liquid composition, a cast solid, a granular form, aparticulate form, a compressed tablet, a gel form, a paste or a slurryform. In one aspect, the activity comprises a cellulase orcellobiohydrolase activity.

In alternative embodiments the invention provides pharmaceuticalcompositions or dietary supplements comprising an enzyme of theinvention, or a cellulase encoded by a nucleic acid of the invention,wherein optionally the enzyme is formulated as a tablet, gel, pill,implant, liquid, spray, powder, food, feed pellet or as an encapsulatedformulation. In one aspect, the activity comprises a cellulase orcellobiohydrolase activity.

In alternative embodiments the invention provides fuels comprising apolypeptide of the invention, or a polypeptide encoded by a nucleic acidof the invention, wherein optionally the fuel is derived from a plantmaterial, which optionally comprises potatoes, soybean (rapeseed),barley, rye, corn, oats, wheat, beets or sugar cane. The plant materialcan be derived from a monocot or a dicot, or a monocot corn, sugarcane,rice, wheat, barley, switchgrass or Miscanthus; or a dicot oilseed crop,soy, canola, rapeseed, flax, cotton, palm oil, sugar beet, peanut, tree,poplar or lupine. The fuel can comprise a bioalcohol, e.g., a bioethanolor a gasoline-ethanol mix, a biomethanol or a gasoline-methanol mix, abiobutanol or a gasoline-butanol mix, or a biopropanol or agasoline-propanol mix. In one aspect, the activity comprises a cellulaseor cellobiohydrolase activity.

In alternative embodiments the invention provides methods for making afuel or alcohol comprising contacting an enzyme of the invention, or acomposition comprising an enzyme of the invention, or a polypeptideencoded by a nucleic acid of the invention, or any one of the mixturesor “cocktails” or products of manufacture of the invention, with abiomass, e.g., a composition comprising a cellulose, a fermentable sugaror polysaccharide, such as a lignocellulosic material. In alternativeembodiments, the composition comprising cellulose or a fermentable sugarcomprises a plant, plant product, plant waste or plant derivative, andthe plant, plant waste or plant product can comprise cane sugar plantsor plant products, beets or sugarbeets, wheat, corn, soybeans, potato,rice or barley. In alternative embodiments, the fuel comprises abioethanol or a gasoline-ethanol mix, a biomethanol or agasoline-methanol mix, a biobutanol or a gasoline-butanol mix, or abiopropanol or a gasoline-propanol mix. The enzyme of the invention ofthe invention can be part of a plant or seed, e.g., a transgenic plantor seed—and in one aspect, the enzyme of the invention is expressed as aheterologous recombinant enzyme in the very biomass (e.g., plant, seed,plant waste) which is targeted for hydrolysis and conversion into a fuelor alcohol by this method of the invention. In one aspect, the activitycomprises cellulase or cellobiohydrolase activity.

In alternative embodiments the invention provides methods for makingbiofuel, e.g., comprising or consisting of a bioalcohol such asbioethanol, biomethanol, biobutanol or biopropanol, or a mixturethereof, comprising contacting a composition comprising an enzyme of theinvention, or a fermentable sugar or lignocellulosic material comprisinga polypeptide of the invention, or a polypeptide encoded by a nucleicacid of the invention, or any one of the mixtures or “cocktails” orproducts of manufacture of the invention, with a biomass, e.g., acomposition comprising a cellulose, a fermentable sugar orpolysaccharide, such as a lignocellulosic material. In alternativeembodiments, the composition comprising the enzyme of the invention,and/or the material to be hydrolyzed, comprises a plant, plant waste,plant product or plant derivative. In alternative embodiments, theplant, plant waste or plant product comprises cane sugar plants or plantproducts (e.g., cane tops), beets or sugarbeets, wheat, corn, soybeans,potato, rice or barley. In one aspect, the plant is a monocot or dicot,or the plant is a monocot corn, sugarcane (including a cane part, e.g.,cane tops), rice, wheat, barley, switchgrass or Miscanthus; or the plantis a dicot oilseed crop, soy, canola, rapeseed, flax, cotton, palm oil,sugar beet, peanut, tree, poplar or lupine. In one aspect, enzyme of theinvention has an activity comprising a cellulase or cellobiohydrolaseactivity. In alternative embodiments the invention provides enzymeensembles, or “cocktail”, for depolymerization of cellulosic andhemicellulosic polymers to metabolizeable carbon moieties comprising apolypeptide of the invention, or a polypeptide encoded by a nucleic acidof the invention. In one aspect, enzyme of the invention has an activitycomprising cellulase or cellobiohydrolase activity. The enzymeensembles, or “cocktails”, of the invention can be in the form of acomposition (e.g., a formulation, liquid or solid), e.g., as a productof manufacture.

In alternative embodiments the invention provides compositions(including products of manufacture, enzyme ensembles, or “cocktails”)comprising (a) a mixture (or “cocktail”, “an enzyme ensemble”, a productof manufacture) of lignocellulosic enzymes, e.g., hemicellulose- andcellulose-hydrolyzing enzymes, including at least one enzyme of thisinvention.

In alternative embodiments the invention provides methods for processinga biomass material comprising lignocellulose comprising contacting acomposition comprising a cellulose, a lignin, or a fermentable sugarwith at least one polypeptide of the invention, or a polypeptide encodedby a nucleic acid of the invention, or an enzyme ensemble, product ofmanufacture or “cocktail” of the invention. In one aspect, the biomassmaterial comprising lignocellulose is derived from an agricultural crop,is a byproduct of a food or a feed production, is a lignocellulosicwaste product, or is a plant residue or a waste paper or waste paperproduct. In alternative embodiments the enzyme of the invention has anactivity comprising a cellobiohydrolase activity. In alternativeembodiments the plant residue(s) comprise grain, seeds, stems, leaves,hulls, husks, corn or corn cobs, corn stover, hay, straw (e.g., a ricestraw or a wheat straw, or any the dry stalk of any cereal plant) and/orgrasses (e.g., Indian grass or switch grass). In alternative embodimentsthe grasses are Indian grass or switch grass, wood, wood chips, woodpulp and sawdust, or wood waste, and optionally the paper wastecomprises discarded or used photocopy paper, computer printer paper,notebook paper, notepad paper, typewriter paper, newspapers, magazines,cardboard and paper-based packaging materials. In one aspect, theprocessing of the biomass material generates a biofuel, e.g., abioalcohol such as bioethanol, biomethanol, biobutanol or biopropanol.

In alternative embodiments the invention provides dairy productscomprising a polypeptide of the invention, or a polypeptide encoded by anucleic acid of the invention, or an enzyme ensemble, product ofmanufacture or “cocktail” of the invention. In one aspect, the dairyproduct comprises a milk, an ice cream, a cheese or a yogurt. In oneaspect, the polypeptide of the invention has a lignocellulosic activity,e.g., an activity comprising a cellulose or cellobiohydrolase activity.

In alternative embodiments the invention provides method for improvingtexture and flavor of a dairy product comprising the following steps:(a) providing a polypeptide of the invention, or a polypeptide encodedby a nucleic acid of the invention, or an enzyme ensemble, product ofmanufacture or “cocktail” of the invention; (b) providing a dairyproduct; and (c) contacting the polypeptide of step (a) and the dairyproduct of step (b) under conditions wherein the polypeptide of theinvention can improve the texture or flavor of the dairy product.

In alternative embodiments the invention provides textiles or fabricscomprising a polypeptide of the invention, or a polypeptide encoded by anucleic acid of the invention, or an enzyme ensemble, product ofmanufacture or “cocktail” of the invention, wherein optionally thetextile or fabric comprises a cellulose-containing fiber. In one aspect,the polypeptide of the invention has a lignocellulosic activity, e.g.,an activity comprising a cellulase or cellobiohydrolase activity.

In alternative embodiments the invention provides methods for treatingsolid or liquid animal waste products comprising the following steps:(a) providing a polypeptide of the invention, or a polypeptide encodedby a nucleic acid of the invention, or an enzyme ensemble, product ofmanufacture or “cocktail” of the invention; (b) providing a solid or aliquid animal waste; and (c) contacting the polypeptide of step (a) andthe solid or liquid waste of step (b) under conditions wherein theprotease can treat the waste. In one aspect, the polypeptide of theinvention has a lignocellulosic activity, e.g., an activity comprising acellulase or cellobiohydrolase activity.

In alternative embodiments the invention provides processed wasteproducts comprising a polypeptide of the invention, or a polypeptideencoded by a nucleic acid of the invention, or an enzyme ensemble,product of manufacture or “cocktail” of the invention. In one aspect,the polypeptide of the invention has a lignocellulosic activity, e.g.,an activity comprising a cellulase or cellobiohydrolase activity.

In alternative embodiments the invention provides disinfectantscomprising a polypeptide having glucose oxidase and/or cellulaseactivity, wherein the polypeptide comprises a sequence of the invention,or a polypeptide encoded by a nucleic acid of the invention, or anenzyme ensemble, product of manufacture or “cocktail” of the invention.In one aspect, the polypeptide of the invention has a lignocellulosicactivity, e.g., an activity comprising a cellulase or cellobiohydrolaseactivity.

In alternative embodiments the invention provides biodefense orbio-detoxifying agents comprising a polypeptide having a lignocellulosicactivity, e.g., a cellulase activity, wherein the polypeptide comprisesa sequence of the invention, or a polypeptide encoded by a nucleic acidof the invention, or an enzyme ensemble, product of manufacture or“cocktail” of the invention. In one aspect, the polypeptide of theinvention has a lignocellulosic activity, e.g., an activity comprising acellulase or cellobiohydrolase activity.

In alternative embodiments the invention provides compositions(including enzyme ensembles and products of manufacture of theinvention) comprising a mixture of enzymes of the invention, e.g.,hemicellulose- and cellulose-hydrolyzing enzymes of the invention, and abiomass material, wherein optionally the biomass material comprises alignocellulosic material derived from an agricultural crop, or thebiomass material is a byproduct of a food or a feed production, or thebiomass material is a lignocellulosic waste product, or the biomassmaterial is a plant residue or a waste paper or waste paper product, orthe biomass material comprises a plant residue, and optionally the plantresidue comprises grains, seeds, stems, leaves, hulls, husks, corn orcorn cobs, corn stover, grasses, wherein optionally grasses are Indiangrass or switch grass, hay or straw (e.g., a rice straw or a wheatstraw, or any the dry stalk of any cereal plant), wood, wood chips, woodpulp, wood waste, and/or sawdust, and optionally the paper wastecomprises discarded or used photocopy paper, computer printer paper,notebook paper, notepad paper, typewriter paper, newspapers, magazines,cardboard and paper-based packaging materials. In alternativeembodiments the polypeptide of the invention has a cellulase orcellobiohydrolase activity.

In alternative embodiments the invention provides methods for processinga biomass material comprising providing enzyme ensembles (“cocktails”)or products of manufacture of the invention, or a mixture ofhemicellulose- and cellulose-hydrolyzing enzymes of the invention,wherein the cellulose-hydrolyzing enzymes comprise at least oneendoglucanase, cellobiohydrolase I, cellobiohydrolase II andβ-glucosidase; and the hemicellulose-hydrolyzing enzymes comprise atleast one xylanase, β-xylosidase and arabinofuranosidase, and contactingthe mixture of enzymes with the biomass material, wherein optionally thebiomass material comprising lignocellulose is derived from anagricultural crop, is a byproduct of a food or a feed production, is alignocellulosic waste product, or is a plant residue or a waste paper orwaste paper product, and optionally the plant residue comprise grains,seeds, stems, leaves, hulls, husks, corn or corn cobs, corn stover,grasses, wherein optionally grasses are Indian grass or switch grass,hay or straw (e.g., a rice straw or a wheat straw, or any the dry stalkof any cereal plant), wood, wood waste, wood chips, wood pulp and/orsawdust, and optionally the paper waste comprises discarded or usedphotocopy paper, computer printer paper, notebook paper, notepad paper,typewriter paper, newspapers, magazines, cardboard and paper-basedpackaging materials, and optionally method further comprises processingthe biomass material to generate a biofuel, e.g., a bioalcohol such asbioethanol, biomethanol, biobutanol or biopropanol, an alcohol and/or asugar (a saccharide). In one aspect, the polypeptide of the inventionhas a lignocellulosic activity, e.g., an activity comprising cellulaseor cellobiohydrolase activity.

In alternative embodiments the invention provides methods for processinga biomass material comprising providing a mixture of enzymes of theinvention (including enzyme ensembles (“cocktails”) or products ofmanufacture of the invention), and contacting the enzyme mixture withthe biomass material, wherein optionally the biomass material comprisinglignocellulose is derived from an agricultural crop, is a byproduct of afood or a feed production, is a lignocellulosic waste product, or is aplant residue or a waste paper or waste paper product, and optionallythe plant residue comprise seeds, stems, leaves, hulls, husks, corn orcorn cobs, corn stover, corn fiber, grasses (e.g. Indian grass or switchgrass), hay, grains, straw (e.g. rice straw or wheat straw or any thedry stalk of any cereal plant), sugarcane bagasse, sugar beet pulp,citrus pulp, and citrus peels, wood, wood thinnings, wood chips, woodpulp, pulp waste, wood waste, wood shavings and sawdust, constructionand/or demolition wastes and debris (e.g. wood, wood shavings andsawdust), and optionally the paper waste comprises discarded or usedphotocopy paper, computer printer paper, notebook paper, notepad paper,typewriter paper, newspapers, magazines, cardboard and paper-basedpackaging materials, and recycled paper materials. In addition, urbanwastes, e.g. the paper fraction of municipal solid waste, municipal woodwaste, and municipal green waste, along with other materials containingsugar, starch, and/or cellulose can be used. Optionally the processingof the biomass material generates a biofuel, e.g., a bioalcohol such asbioethanol, biomethanol, biobutanol or biopropanol. In one aspect, thepolypeptide of the invention has a lignocellulosic activity, e.g., anactivity comprising a cellulase or cellobiohydrolase activity.

The details of one or more aspects of the invention are set forth in theaccompanying drawings and the description below. Other features,objects, and advantages of the invention will be apparent from thedescription and drawings, the numbered paragraphs preceding the claims,and from the claims themselves.

All publications, patents, patent applications, GenBank sequences andATCC deposits, cited herein are hereby expressly incorporated byreference for all purposes.

5. BRIEF DESCRIPTION OF THE DRAWINGS

The following drawings are illustrative of aspects of the invention andare not meant to limit the scope of the invention as encompassed by theparagraphs.

FIG. 1A-1F shows an alignment of variant CBH I polypeptide sequences ofSEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ IDNO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ IDNO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ IDNO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ IDNO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ IDNO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58; SEQ ID NO:60, SEQ IDNO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ IDNO:72, SEQ ID NO:74, SEQ ID NO:76, SEQ ID NO:78, SEQ ID NO:80, SEQ IDNO:82, SEQ ID NO:84, SEQ ID NO:86, SEQ ID NO:88, SEQ ID NO:90, SEQ IDNO:92, SEQ ID NO:94, SEQ ID NO:96, SEQ ID NO:98, SEQ ID NO:100, SEQ IDNO:102, SEQ ID NO:104, SEQ ID NO:106, SEQ ID NO:108, SEQ ID NO:110, SEQID NO:112, SEQ ID NO:114, SEQ ID NO:116, SEQ ID NO:118, SEQ ID NO:120,SEQ ID NO:122, SEQ ID NO:124, SEQ ID NO:126, SEQ ID NO:128, SEQ IDNO:130, SEQ ID NO:132, SEQ ID NO:134, and/or SEQ ID NO:136. SEQ IDNO:60, 94, 120 and 134 are “wild type” BD29555 sequences; the amino acidsubstitutions (include the substitution of the 9-amino acid substrateentry loop at positions 120-128 of BD29555 with a longer (13-amino acidloop) are underlined. FIG. 1G-1U shows an alignment of variant CBH Ipolypeptide sequences of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ IDNO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ IDNO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ IDNO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ IDNO:37,SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ IDNO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ IDNO:57: SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ IDNO:67, SEQ ID NO:69, SEQ ID NO:71, SEQ ID NO:73, SEQ ID NO:75, SEQ IDNO:77, SEQ ID NO:79, SEQ ID NO:81, SEQ ID NO:83, SEQ ID NO:85, SEQ IDNO:87, SEQID NO:89, SEQ ID NO:91, SEQ ID NO:93, SEQ ID NO:95, SEQ IDNO:97, SEQ ID NO:99, SEQ ID NO:101, SEQ ID NO:103, SEQ ID NO:105, SEQ IDNO:107, SEQ ID NO:109, SEQ ID NO:111, SEQ ID NO:113, SEQ ID NO:115, SEQID NO:117, SEQ ID NO:119, SEQ ID NO:121, SEQ ID NO:123, SEQ ID NO:125,SEQ ID NO:127, SEQ ID NO:129, SEQ ID NO:131, SEQID NO:133, and/or SEQ IDNO:135.

6. DETAILED DESCRIPTION OF THE INVENTION

In one aspect, the invention provides polypeptides having anylignocellulolytic (lignocellulosic) activity, including ligninolytic andcellulolytic activity, including, e.g., a cellulase and/or acellobiohydrolase (cbhl) (e.g., an exo-cellobiohydrolase, e.g., havingan “exo” activity that can processively release cellobiose units β-1,4glucose-glucose disaccharide) activity, polynucleotides encoding thesepolypeptides, and methods of making and using these polynucleotides andpolypeptides. In one aspect, the invention provides polypeptides havinga lignocellulosic activity, e.g., cellulase and/or a cellobiohydrolaseactivity, including enzymes that convert soluble oligomers tofermentable monomeric sugars in the saccharification of biomass. In oneaspect, an activity of a polypeptide of the invention comprisesenzymatic hydrolysis of (to degrade) soluble cellooligsaccharides and/oroligomers into monomers (e.g. xylose, arabinose or glucose). In oneaspect, the invention provides thermostable and thermotolerant forms ofpolypeptides of the invention. The polypeptides of the invention can beused in a variety of pharmaceutical, agricultural and industrialcontexts.

In one aspect, the invention provides a lignocellulosic enzyme, e.g., acellulase or a cellobiohydrolase (cbhl) (e.g., an exo-cellobiohydrolase,e.g., having an “exo” activity that can processively release cellobioseunits β-1,4 glucose-glucose disaccharide), with an increased catalyticrate, thus improving the process of substrate hydrolysis. In one aspect,the invention provides a lignocellulosic enzyme active under relativelyextreme conditions, e.g., high or low temperatures or salt conditions,and/or acid or basic conditions, including pHs and temperatures higheror lower than physiologic. This increased efficiency in catalytic rateleads to an increased efficiency in producing sugars that, in oneembodiment, are used by microorganisms for ethanol production. In oneaspect, microorganisms generating enzyme of the invention are used withsugar hydrolyzing, e.g., ethanol-producing, microorganisms. Thus, theinvention provides methods for biofuel, e.g., a bioalcohol such asbioethanol, biomethanol, biobutanol or biopropanol, production andmaking “clean fuels” based on alcohols, e.g., for transportation usingbiofuels.

In one aspect the invention provides compositions (e.g., enzymepreparations, feeds, drugs, dietary supplements) comprising the enzymes,polypeptides or polynucleotides of the invention. These compositions canbe formulated in a variety of forms, e.g., as liquids, gels, pills,tablets, sprays, powders, food, feed pellets or encapsulated forms,including nanoencapsulated forms.

Assays for measuring cellulase activity, e.g., endoglucanase, acellobiohydrolase (cbhl) (e.g., an exo-cellobiohydrolase, e.g., havingan “exo” activity that can processively release cellobiose units β-1,4glucose-glucose disaccharide) activity, e.g., for determining if apolypeptide has cellulase activity, e.g., cellobiohydrolase activity,are well known in the art and are within the scope of the invention;see, e.g., Baker W L, Panow A, Estimation of cellulase activity using aglucose-oxidase-Cu(II) reducing assay for glucose, J Biochem BiophysMethods. 1991 December, 23(4):265-73; Sharrock K R, Cellulase assaymethods: a review, J Biochem Biophys Methods. 1988 October,17(2):81-105; Carder J H, Detection and quantitation of cellulase byCongo red staining of substrates in a cup-plate diffusion assay, AnalBiochem. 1986 Feb. 15, 153(1):75-9; Canevascini G., A cellulase assaycoupled to cellobiose dehydrogenase, Anal Biochem. 1985 June,147(2):419-27; Huang J S, Tang J, Sensitive assay for cellulase anddextranase. Anal Biochem. 1976 June, 73(2):369-77.

The pH of reaction conditions utilized by the invention is anothervariable parameter for which the invention provides. In certain aspects,the pH of the reaction is conducted in the range of about 3.0 or less toabout 9.0 or more, and in one embodiment an enzyme of the invention isactive under such acidic or basic conditions. In other aspects, aprocess of the invention is practiced at a pH of about 4.0, 4.5, 5.0,5.5, 6.0, 6.5, 7.5, 8.0, 8.5, 9.0 or 9.5, or more, and in one embodimentan enzyme of the invention is active under such acidic or basicconditions. Reaction conditions conducted under alkaline conditions alsocan be advantageous, e.g., in some industrial or pharmaceuticalapplications of enzymes of the invention.

The invention provides compositions, including pharmaceuticals,additives and supplements, comprising a lignocellulosic enzyme of theinvention, including polypeptides having a cellulase or acellobiohydrolase (cbhl) (e.g., an exo-cellobiohydrolase, e.g., havingan “exo” activity that can processively release cellobiose units β-1,4glucose-glucose disaccharide) activity, in a variety of forms andformulations. In the methods of the invention, the lignocellulosicenzymes of the invention also are used in a variety of forms andformulations. For example, purified the lignocellulosic enzyme can beused in enzyme preparations deployed in a biofuel, e.g., a bioalcoholsuch as bioethanol, biomethanol, biobutanol or biopropanol, productionor in pharmaceutical, food, feed or dietary aid applications.Alternatively, the enzymes of the invention can be used directly orindirectly in processes to produce a biofuel, e.g., a bioalcohol such asbioethanol, biomethanol, biobutanol or biopropanol, make clean fuels,process biowastes, process foods, chemicals, pharmaceuticals,supplements, liquids, foods or feeds, and the like.

Alternatively, the lignocellulosic enzyme, e.g., a cellulase or acellobiohydrolase (cbhl) (e.g., an exo-cellobiohydrolase, e.g., havingan “exo” activity that can processively release cellobiose units β-1,4glucose-glucose disaccharide) polypeptide of the invention can beexpressed in a microorganism (including bacterial, yeast, viruses, fungiand the like) using procedures known in the art. The microorganismexpressing an enzyme of the invention can live on or in a plant, plantpart (e.g., a seed) or an organism. In other aspects, thelignocellulosic enzyme of the invention can be immobilized on a solidsupport prior to use in the methods of the invention. Methods forimmobilizing enzymes on solid supports are commonly known in the art,for example J. Mol. Cat. B: Enzymatic 6 (1999) 29-39; Chivata et al.Biocatalysis: Immobilized cells and enzymes, J. Mol. Cat. 37 (1986)1-24: Sharma et al., Immobilized Biomaterials Techniques andApplications, Angew. Chem. Int. Ed. Engl. 21 (1982) 837-54: Laskin(Ed.), Enzymes and Immobilized Cells in Biotechnology.

6.1. Nucleic Acids, Probes and Inhibitory Molecules

In alternative embodiments, the invention provides nucleic acidsencoding the polypeptides of the invention, e.g., a cellobiohydrolase(cbhl) (e.g., an exo-cellobiohydrolase, e.g., having an “exo” activitythat can processively release cellobiose units β-1,4 glucose-glucosedisaccharide). The invention also provides expression cassettes, vectorssuch as expression or cloning vectors, cloning vehicles such as a viralvector, a plasmid, a phage, a phagemid, a cosmid, a fosmid, abacteriophage or an artificial chromosome, which can comprise, or havecontained therein, a nucleic acid of the invention.

The invention also includes methods for discovering new enzyme sequencesusing the nucleic acids of the invention. Also provided are methods formodifying the nucleic acids of the invention by, e.g., Gene SiteSaturation Mutagenesis^(SM) technology, GeneReassembly^(SM) technology,and/or Tailored Multi-Site Combinatorial Asembly^(SM) technology.

In alternative embodiments, the invention provides a genus of nucleicacids based on the exemplary nucleic acids of the invention comprising:

The exemplary SEQ ID NO:1 encoding a polypeptide (e.g., the exemplarySEQ ID NO:2 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCCATACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:2 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNAHTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:3 encoding a polypeptide (e.g., the exemplarySEQ ID NO:4 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCGAGACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:4 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNAETGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:5 encoding a polypeptide (e.g., the exemplarySEQ ID NO:6 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCAAGTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:6 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPKSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:7 encoding a polypeptide (e.g., the exemplarySEQ ID NO:8 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGATATGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:8 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGYGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:9 encoding a polypeptide (e.g., the exemplarySEQ ID NO:10 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGAGTGGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:10 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGVGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:11 encoding a polypeptide (e.g., the exemplarySEQ ID NO:12 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTTCGTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTG TAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:12 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAASWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:13 encoding a polypeptide (e.g., the exemplarySEQ ID NO:14 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTAAGACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:14 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPKTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:15 encoding a polypeptide (e.g., the exemplarySEQ ID NO:16 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCCTTACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:16 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICLTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:17 encoding a polypeptide (e.g., the exemplarySEQ ID NO:18 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCATTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:18 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPILSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:19 encoding a polypeptide (e.g., the exemplarySEQ ID NO:20 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCGGGCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:20 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSGLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:21 encoding a polypeptide (e.g., the exemplarySEQ ID NO:22 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCGGGTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:22 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLGCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:23 encoding a polypeptide (e.g., the exemplarySEQ ID NO:24 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACGCTAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:24 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNAKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:25 encoding a polypeptide (e.g., the exemplarySEQ ID NO:26 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCGGTCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCC TTACTACTCTCAATGTTTGTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:26 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVGHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQC

The exemplary SEQ ID NO:27 encoding a polypeptide (e.g., the exemplarySEQ ID NO:28 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCCCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCTCTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCC TTACTACTCTCAATGTTTGTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:28 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSPNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVSDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:29 encoding a polypeptide (e.g., the exemplarySEQ ID NO:30 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACCAGGGCACATCCTCCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGGTCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCC TTACTACTCTCAATGTTTGTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:30 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDQGTSSGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEVSTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:31 encoding a polypeptide (e.g., the exemplarySEQ ID NO:32 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCCGTCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCC TTACTACTCTCAATGTTTGTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:32 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGRLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:33 encoding a polypeptide (e.g., the exemplarySEQ ID NO:34 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGAGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCCTTGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCC TTACTACTCTCAATGTTTGTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:34 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLLEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:35 encoding a polypeptide (e.g., the exemplarySEQ ID NO:36 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTAGTAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCC TTACTACTCTCAATGTTTGTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:36 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVSNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:37 encoding a polypeptide (e.g., the exemplarySEQ ID NO:38 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCGATATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCC TTACTACTCTCAATGTTTGTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:38 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSDISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:39 encoding a polypeptide (e.g., the exemplarySEQ ID NO:40 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAGATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCGCTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCTGTGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATG TTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:40 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCRSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVADFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVCGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:41 encoding a polypeptide (e.g., the exemplarySEQ ID NO:42 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGATAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCC TTACTACTCTCAATGTTTGTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:42 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSDNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:43 encoding a polypeptide (e.g., the exemplarySEQ ID NO:44 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAGTTGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCC TTACTACTCTCAATGTTTGTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:44 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGVVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:45 encoding a polypeptide (e.g., the exemplarySEQ ID NO:46 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTGTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCC TTACTACTCTCAATGTTTGTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:46 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDLCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:47 encoding a polypeptide (e.g., the exemplarySEQ ID NO:48 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTATTTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCC TTACTACTCTCAATGTTTGTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:48 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETISFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:49 encoding a polypeptide (e.g., the exemplarySEQ ID NO:50 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACCGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:50 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHRGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQC

The exemplary SEQ ID NO:51 encoding a polypeptide (e.g., the exemplarySEQ ID NO:52 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGAGTGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:52 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMSAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:53 encoding a polypeptide (e.g., the exemplarySEQ ID NO:54 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGTGGGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:54 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRWGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:55 encoding a polypeptide (e.g., the exemplarySEQ ID NO:56 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCGGTTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:56 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFGSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:57 encoding a polypeptide (e.g., the exemplarySEQ ID NO:58 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAAGACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:58 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSKTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:59 encoding a polypeptide (e.g., the exemplarySEQ ID NO:60 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:60 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:61 encoding a polypeptide (e.g., the exemplarySEQ ID NO:62 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACAATGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:62 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYNGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:63 encoding a polypeptide (e.g., the exemplarySEQ ID NO:62 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCAGTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:64 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFSTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:65 encoding a polypeptide (e.g., the exemplarySEQ ID NO:66 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCACTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:66 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFTTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:67 encoding a polypeptide (e.g., the exemplarySEQ ID NO:68 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCAATAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:68 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSNNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:69 encoding a polypeptide (e.g., the exemplarySEQ ID NO:70 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCAACGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:70 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSTRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:71 encoding a polypeptide (e.g., the exemplarySEQ ID NO:72 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTGTTTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:72 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGVYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:73 encoding a polypeptide (e.g., the exemplarySEQ ID NO:74 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAGCTCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGCCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:74 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAEAHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSANMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:75 encoding a polypeptide (e.g., the exemplarySEQ ID NO:76 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGACTATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:76 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLTMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:77 encoding a polypeptide (e.g., the exemplarySEQ ID NO:78 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACGATTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:78 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDDSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:79 encoding a polypeptide (e.g., the exemplarySEQ ID NO:80 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGATAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:80 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSDNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:81 encoding a polypeptide (e.g., the exemplarySEQ ID NO:82 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACCCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGCCATGAGTTTGTGGGACGACTACTCCGCTAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTGCCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:82 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLAMSLWDDYSANMLWLDSTYPTNATGAPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:83 encoding a polypeptide (e.g., the exemplarySEQ ID NO:84 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGACTTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:84 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMTWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:85 encoding a polypeptide (e.g., the exemplarySEQ ID NO:86 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTTATACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:86 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSYTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:87 encoding a polypeptide (e.g., the exemplarySEQ ID NO:88 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGTCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACGTCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGCCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCTGGACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:88 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNVNTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSANMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASWTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:89 encoding a polypeptide (e.g., the exemplarySEQ ID NO:90 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCATGAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:90 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTMSGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:91 encoding a polypeptide (e.g., the exemplarySEQ ID NO:92 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATTAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGCCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGACTTGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:92 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSANMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGLAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:93 encoding a polypeptide (e.g., the exemplarySEQ ID NO:94 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:94 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:95 encoding a polypeptide (e.g., the exemplarySEQ ID NO:96 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTCTGCAGGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCGCCCAGAACTGCTACGATGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCCAGCAGGGCCCCTACTCCAAGAACGTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGT AA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO: 96 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTLQAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTAQNCYDGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVQQGPYSKNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:97 encoding a polypeptide (e.g., the exemplarySEQ ID NO:98 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTCTGACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTGGACCAACTGCTACGATGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCCAGCAGGGCCCCTACTCCAAGAACGTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGT AA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO: 98 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTLTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTWTNCYDGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVQQGPYSKNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:99 encoding a polypeptide (e.g., the exemplarySEQ ID NO:100 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTACCAGAACTGCTACACCGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCCAGCAGGGCCCCTACTCCAAGAACGTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGT AA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO: 100 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTYQNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVQQGPYSKNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:101 encoding a polypeptide (e.g., the exemplarySEQ ID NO:102 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTCTGTGGGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCCAGCAGGGCCCCTACTCCAAGAACGTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGT AA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:102 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTLWAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVQQGPYSKNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:103 encoding a polypeptide (e.g., the exemplarySEQ ID NO:104 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTACCAGGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCACCAAGGGCTCCTTCTCCTCCAACATCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGT AA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:104 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYQAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTKGSFSSNIGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:105 encoding a polypeptide (e.g., the exemplarySEQ ID NO:106 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTCAGCAGGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTACACCAACTGCTACGATGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCACCCAGTCCGCCCAGAAGAACGTCGGCGCCCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:106 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTQQAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTYTNCYDGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTQSAQKNVGARTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:107 encoding a polypeptide (e.g., the exemplarySEQ ID NO:108 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTGCCTACGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTACTACAACTGCTACGATGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCACCGGCTCCAACGTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:108 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTAYAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTYYNCYDGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRGVGPFNSTFSGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:109 encoding a polypeptide (e.g., the exemplarySEQ ID NO:110 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTCAGCAGGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTACTACAACTGCTACGATGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCACCGGCTCCAACGTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:110 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTQQAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTYYNCYDGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:111 encoding a polypeptide (e.g., the exemplarySEQ ID NO:112 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTACTGGGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTCCTGGAACTGCTACGATGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCACCGGCTCCAACGTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:112 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYWAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSWNCYDGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:113 encoding a polypeptide (e.g., the exemplarySEQ ID NO:114 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTGCCCAGGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTCCTACAACTGCTACGATGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCACCGGCTCCAACGTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:114 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTAQAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSYNCYDGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:115 encoding a polypeptide (e.g., the exemplarySEQ ID NO:116 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTGGCAGAACTGCTACACCGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCCAGCAGGGCCCCTACTCCAAGAACGTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGT AA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:116 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTWQNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVQQGPYSKNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:117 encoding a polypeptide (e.g., the exemplarySEQ ID NO:118 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTCTGTACGCTGCAAACCCATCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTCCACCAACTGCTACGATGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCCAGCAGGGCCCCTACTCCAAGAACGTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGT AA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:118 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTLYAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYDGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVQQGPYSKNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:119 encoding a polypeptide (e.g., the exemplarySEQ ID NO:120 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGATGATTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:120 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:121 encoding a polypeptide (e.g., the exemplarySEQ ID NO:122 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCGGGTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCAAGTCCAACAACGCCCATACTGGATATGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCGATATCTCCGGAGTCAGCGGAGTTGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGTGGGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:122 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLGCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPKSNNAHTGYGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSDISGVSGVVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRWGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:123 encoding a polypeptide (e.g., the exemplarySEQ ID NO:124 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCCATACTGGATATGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCGATATCTCCGGAGTCAGCGGAGTTGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGAGTGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGTGGGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCC TTACTACTCTCAATGTTTGTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:124 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNAHTGYGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSDISGVSGVVINSDFCDAEISTFGETASFSKHGGLAKMGAGMSAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRWGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:125 encoding a polypeptide (e.g., the exemplarySEQ ID NO:126 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCCTTGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCGATATCTCCGGAGTCAGCGGAGTTGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCC TTACTACTCTCAATGTTTGTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:126 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLLEIRRYYVQNGVVIPQPSSDISGVSGVVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:127 encoding a polypeptide (e.g., the exemplarySEQ ID NO:128 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGATATGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACCAGGGCACATCCACCGGCCGTCTCCTTGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCGATATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGAGTGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:128 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGYGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDQGTSTGRLLEIRRYYVQNGVVIPQPSSDISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMSAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:129 encoding a polypeptide (e.g., the exemplarySEQ ID NO:130 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCGGGTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCAAGTCCAACAACGCCCATACTGGATATGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTAGTAACGGTGTTGTCATCCCCCAGCCTTCCTCCGATATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGAGTGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:130 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLGCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPKSNNAHTGYGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVSNGVVIPQPSSDISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMSAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:131 encoding a polypeptide (e.g., the exemplarySEQ ID NO:132 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGAGTGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGTGGGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:132 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMSAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRWGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:133 encoding a polypeptide (e.g., the exemplarySEQ ID NO:134 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAA

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:134 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAARGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The exemplary SEQ ID NO:135 encoding a polypeptide (e.g., the exemplarySEQ ID NO:136 and enzymatically active fragments thereof) having acellobiohydrolase activity:

ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCTACAGCTCCGATAAGTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTAAGGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTT GTAG

A nucleic acid encoding a polypeptide having a cellobiohydrolaseactivity comprising or consisting of the exemplary SEQ ID NO:136 (orenzymatically active fragments thereof):

MSALNSFNMYKSALILGSLLATAGAQQIGTYTAETHPSLSWSTCKSGGSCTTNSGAITLDANWRWVHGVNTSTNCYTGNTWNTAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVGSRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGVSKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSSNNANTGLGNHGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDKYAGTCDPDGCDFNPYRLGVTDFYGSGKTVDTTKPITVVTQFVTDDGTSTGTLSEIRRYYVQNGVVIPQPSSKISGVSGNVINSDFCDAEISTFGETASFSKHGGLAKMGAGMEAGMVLVMSLWDDYSVNMLWLDSTYPTNATGTPGAAKGSCPTTSGDPKTVESQSGSSYVTFSDIRVGPFNSTFSGGSSTGGSSTTTASGTTTTKASSTSTSSTSTGTGVAAHWGQCGGQGWTGPTTCASGTTCTVVNPYYSQCL

The nucleic acids of the invention can be made, isolated and/ormanipulated by, e.g., cloning and expression of cDNA libraries,amplification of message or genomic DNA by PCR, and the like. Inpracticing the methods of the invention, homologous genes can bemodified by manipulating a template nucleic acid, as described herein.The invention can be practiced in conjunction with any method orprotocol or device known in the art, which are well described in thescientific and patent literature.

6.2. General Techniques

The nucleic acids used to practice this invention, whether RNA, iRNA,miRNA, antisense nucleic acid, cDNA, genomic DNA, vectors, viruses orhybrids thereof, may be isolated from a variety of sources, geneticallyengineered, amplified, and/or expressed/generated recombinantly.Recombinant polypeptides generated from these nucleic acids can beindividually isolated or cloned and tested for a desired activity. Anyrecombinant expression system can be used, including bacterial,mammalian, yeast, insect or plant cell expression systems.

Alternatively, these nucleic acids can be synthesized in vitro bywell-known chemical synthesis techniques, as described in, e.g., Adams(1983) J. Am. Chem. Soc. 105:661; Belousov (1997) Nucleic Acids Res.25:3440-3444; Frenkel (1995) Free Radic. Biol. Med. 19:373-380; Blommers(1994) Biochemistry 33:7886-7896; Narang (1979) Meth. Enzymol. 68:90;Brown (1979) Meth. Enzymol. 68:109; Beaucage (1981) Tetra. Lett.22:1859; U.S. Pat. No. 4,458,066.

Techniques for the manipulation of nucleic acids, such as, e.g.,subcloning, labeling probes (e.g., random-primer labeling using Klenowpolymerase, nick translation, amplification), sequencing, hybridizationand the like are well described in the scientific and patent literature,see, e.g., Sambrook, ed., MOLECULAR CLONING: A LABORATORY MANUAL (2NDED.), Vols. 1-3, Cold Spring Harbor Laboratory, (1989); CURRENTPROTOCOLS IN MOLECULAR BIOLOGY, Ausubel, ed. John Wiley & Sons, Inc.,New York (1997); LABORATORY TECHNIQUES IN BIOCHEMISTRY AND MOLECULARBIOLOGY: HYBRIDIZATION WITH NUCLEIC ACID PROBES, Part I. Theory andNucleic Acid Preparation, Tijssen, ed. Elsevier, N.Y. (1993).

Another useful means of obtaining and manipulating nucleic acids used topractice the methods of the invention is to clone from genomic samples,and, if desired, screen and re-clone inserts isolated or amplified from,e.g., genomic clones or cDNA clones. Sources of nucleic acid used in themethods of the invention include genomic or cDNA libraries contained in,e.g., mammalian artificial chromosomes (MACs), see, e.g., U.S. Pat. Nos.5,721,118; 6,025,155; human artificial chromosomes, see, e.g., Rosenfeld(1997) Nat. Genet. 15:333-335; yeast artificial chromosomes (YAC);bacterial artificial chromosomes (BAC); P1 artificial chromosomes, see,e.g., Woon (1998) Genomics 50:306-316; P1-derived vectors (PACs), see,e.g., Kern (1997) Biotechniques 23:120-124; cosmids, recombinantviruses, phages or plasmids.

In alternative aspects, the phrases “nucleic acid” or “nucleic acidsequence” refer to an oligonucleotide, nucleotide, polynucleotide, or toa fragment of any of these, to DNA or RNA (e.g., mRNA, rRNA, tRNA) ofgenomic or synthetic origin which may be single-stranded ordouble-stranded and may represent a sense or antisense strand, topeptide nucleic acid (PNA), or to any DNA-like or RNA-like material,natural or synthetic in origin, including, e.g., iRNA,ribonucleoproteins (e.g., iRNPs). The term encompasses nucleic acids,i.e., oligonucleotides, containing known analogues of naturalnucleotides. The term also encompasses nucleic-acid-like structures withsynthetic backbones, see e.g., Mata (1997) Toxicol. Appl. Pharmacol.144:189-197; Strauss-Soukup (1997) Biochemistry 36:8692-8698; Samstag(1996) Antisense Nucleic Acid Drug Dev 6:153-156.

In one aspect, a nucleic acid encoding a polypeptide of the inventionfurther comprises a sequence encoding a leader sequence assembled inappropriate phase with the polypeptide to direct secretion of thetranslated polypeptide or fragment thereof.

The invention provides fusion proteins and nucleic acids encoding them.A polypeptide of the invention can be fused to a heterologous peptide orpolypeptide, such as N-terminal identification peptides which impartdesired characteristics, such as increased stability or simplifiedpurification. Peptides and polypeptides of the invention can also besynthesized and expressed as fusion proteins with one or more additionaldomains linked thereto for, e.g., producing a more immunogenic peptide,to more readily isolate a recombinantly synthesized peptide, to identifyand isolate antibodies and antibody-expressing B cells, and the like.Detection and purification facilitating domains include, e.g., metalchelating peptides such as polyhistidine tracts and histidine-tryptophanmodules that allow purification on immobilized metals, protein A domainsthat allow purification on immobilized immunoglobulin, and the domainutilized in the FLAGS extension/affinity purification system (ImmunexCorp, Seattle Wash.). The inclusion of a cleavable linker sequences suchas Factor Xa or enterokinase (Invitrogen, San Diego Calif.) between apurification domain and the motif-comprising peptide or polypeptide tofacilitate purificationTranscriptional and translational controlsequences

The invention provides nucleic acid (e.g., DNA) sequences of theinvention operatively linked to expression (e.g., transcriptional ortranslational) control sequence(s), e.g., promoters or enhancers, todirect or modulate RNA synthesis/expression. The expression controlsequence can be in an expression vector.

Any promoter known to control expression of genes in prokaryotic oreukaryotic cells or their viruses can be used.

6.3. Expression Vectors and Cloning Vehicles

The invention provides expression systems, e.g., expression cassettes,vectors, cloning vehicles and the like, comprising nucleic acids of theinvention, e.g., sequences encoding polypeptides of the invention, forexpression, and over-expression, of the polypeptides of the invention(and nucleic acids, e.g., antisense). Expression vectors and cloningvehicles of the invention can comprise viral particles, baculovirus,phage, plasmids, phagemids, cosmids, fosmids, bacterial artificialchromosomes, viral DNA (e.g., vaccinia, adenovirus, foul pox virus,pseudorabies and derivatives of SV40), P1-based artificial chromosomes,yeast plasmids, yeast artificial chromosomes, and any other vectorsspecific for specific hosts of interest, such as bacillus, Aspergillusand yeast. In alternative embodiments, nucleic acids of the inventionare expressed in a Pichia, e.g., a Pichia pastoris, aSchizosaccharomyces, e.g., a Schizosaccharomyces pombe, and/or aPseudomonas, e.g., a Pseudomonas fluorescens; e.g., to express apolypeptide of the invention.

Vectors of the invention can include chromosomal, non-chromosomal andsynthetic DNA sequences. Large numbers of suitable vectors are known tothose of skill in the art, and are commercially available. Any plasmidor other vector can be used, e.g., those replicable and viable in adesired host. Low copy number or high copy number vectors may beemployed in practicing the present invention.

In one aspect, expression cassettes of the invention comprise a sequenceof the invention and a nucleotide sequence which is capable of affectingexpression of a structural gene (i.e., a protein coding sequence, suchas a polypeptide of the invention) in a host compatible with suchsequences. Expression cassettes include at least a promoter operablylinked with the polypeptide coding sequence; and, optionally, with othersequences, e.g., transcription termination signals. Additional factorsnecessary or helpful in effecting expression may also be used, e.g.,enhancers. Expression cassettes used to practice the invention includeplasmids, expression vectors, recombinant viruses, any form ofrecombinant “naked DNA” vector, and the like. In one aspect, a “vector”comprises a nucleic acid that can infect, transfect, transiently orpermanently transduce a cell. A vector can be a naked nucleic acid, or anucleic acid complexed with protein or lipid. The vector optionallycomprises viral or bacterial nucleic acids and/or proteins, and/ormembranes (e.g., a cell membrane, a viral lipid envelope, etc.). In oneaspect, vectors include, but are not limited to, replicons (e.g., RNAreplicons, bacteriophages) to which fragments of DNA may be attached andbecome replicated. In one aspect, vectors include, but are not limitedto RNA, autonomous self-replicating circular or linear DNA or RNA (e.g.,plasmids, viruses, and the like, see, e.g., U.S. Pat. No. 5,217,879),and includes both the expression and non-expression plasmids. Where arecombinant microorganism or cell culture is described as hosting an“expression vector” this includes both extra-chromosomal circular andlinear DNA and DNA that has been incorporated into the hostchromosome(s). Where a vector is being maintained by a host cell, thevector may either be stably replicated by the cells during mitosis as anautonomous structure, or is incorporated within the host's genome.

In one aspect, the expression vectors contain one or more selectablemarker genes to permit selection of host cells containing the vector.

6.4. Host Cells and Transformed Cells

The invention also provides a transformed cell comprising a nucleic acidsequence of the invention, e.g., a sequence encoding a polypeptide ofthe invention, or comprising an expression cassette, vector, cloningvehicle, expression vector, or cloning vector of the invention. The hostcell may be any of the host cells familiar to those skilled in the art,including prokaryotic cells, eukaryotic cells, such as bacterial cells,fungal cells, yeast cells, mammalian cells, insect cells, or plantcells. Exemplary bacterial cells include any species within the generaEscherichia, Bacillus, Streptomyces, Salmonella, Pseudomonas,Lactococcus, and Staphylococcus, including, e.g., Escherichia coli,Lactococcus lactis, Bacillus subtilis, Bacillus cereus, Salmonellatyphimurium, Pseudomonas fluorescens. Exemplary fungal cells include anyspecies of Aspergillus, including Aspergillus niger. Exemplary yeastcells include any species of Pichia, Saccharomyces, Schizosaccharomyces,or Schwanniomyces, including Pichia pastoris, Saccharomyces cerevisiae,or Schizosaccharomyces pombe. Exemplary insect cells include any speciesof Spodoptera or Drosophila, including Drosophila S2 and Spodoptera Sf9.Exemplary insect cells include Drosophila S2 and Spodoptera Sf9.Exemplary yeast cells include Pichia pastoris, Saccharomyces cerevisiaeor Schizosaccharomyces pombe. Exemplary animal cells include CHO, COS orBowes melanoma or any mouse or human cell line. The selection of anappropriate host is within the abilities of those skilled in the art.

The vector may be introduced into the host cells using any of a varietyof techniques, including transformation, transfection, transduction,viral infection, gene guns, or Ti-mediated gene transfer. Particularmethods include calcium phosphate transfection, DEAE-Dextran mediatedtransfection, lipofection, or electroporation (Davis, L., Dibner, M.,Battey, I., Basic Methods in Molecular Biology, (1986)).

Where appropriate, the engineered host cells can be cultured inconventional nutrient media modified as appropriate for activatingpromoters, selecting transformants or amplifying the genes of theinvention. Following transformation of a suitable host strain and growthof the host strain to an appropriate cell density, the selected promotermay be induced by appropriate means (e.g., temperature shift or chemicalinduction) and the cells may be cultured for an additional period toallow them to produce the desired polypeptide or fragment thereof.

Cell-free translation systems can also be employed to produce apolypeptide of the invention. Cell-free translation systems can usemRNAs transcribed from a DNA construct comprising a promoter operablylinked to a nucleic acid encoding the polypeptide or fragment thereof.In some aspects, the DNA construct may be linearized prior to conductingan in vitro transcription reaction. The transcribed mRNA is thenincubated with an appropriate cell-free translation extract, such as arabbit reticulocyte extract, to produce the desired polypeptide orfragment thereof.

The nucleic acids of the invention can be expressed, or overexpressed,in any in vitro or in vivo expression system. Any cell culture systemscan be employed to express, or over-express, recombinant protein,including bacterial, insect, yeast, fungal or mammalian cultures.Over-expression can be effected by appropriate choice of promoters,enhancers, vectors (e.g., use of replicon vectors, dicistronic vectors(see, e.g., Gurtu (1996) Biochem. Biophys. Res. Commun. 229:295-8)),media, culture systems and the like. In one aspect, gene amplificationusing selection markers, e.g., glutamine synthetase (see, e.g., Sanders(1987) Dev. Biol. Stand. 66:55-63), in cell systems are used tooverexpress the polypeptides of the invention.

6.5. Amplification of Nucleic Acids

In practicing the invention, nucleic acids encoding the polypeptides ofthe invention, or modified nucleic acids, can be reproduced by, e.g.,amplification. The invention provides amplification primer sequencepairs for amplifying nucleic acids encoding polypeptides with e.g., acellulase or a cellobiohydrolase activity, or subsequences thereof,where the primer pairs are capable of amplifying nucleic acid sequencesincluding an exemplary sequence of the invention, and at least one ofthe specific sequence modifications set forth above. One of skill in theart can design amplification primer sequence pairs for any part of orthe full length of these sequences; for example:

6.6. Determining the Degree of Sequence Identity

The invention provides an isolated, synthetic or recombinant nucleicacid comprising a nucleic acid sequence having at least 70%, 71%, 72%,73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%,87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or moresequence identity to an exemplary sequence of the invention, andincluding at least one of the specifically enumerated modifications toan exemplary sequence of the invention discussed above. In one aspect,the extent of sequence identity (homology) may be determined using anycomputer program and associated parameters, including those describedherein, such as BLAST 2.2.2. or FASTA version 3.0t78, with the defaultparameters.

Various sequence comparison programs identified herein are used in thisaspect of the invention. Protein and/or nucleic acid sequence identities(homologies) may be evaluated using any of the variety of sequencecomparison algorithms and programs known in the art. Such algorithms andprograms include, but are not limited to, TBLASTN, BLASTP, FASTA,TFASTA, and CLUSTALW (Pearson and Lipman, Proc. Natl. Acad. Sci. USA85(8):2444-2448, 1988; Altschul et al., J. Mol. Biol. 215(3):403-410,1990; Thompson et al., Nucleic Acids Res. 22(2):4673-4680, 1994; Higginset al., Methods Enzymol. 266:383-402, 1996; Altschul et al., J. Mol.Biol. 215(3):403-410, 1990; Altschul et al., Nature Genetics 3:266-272,1993.

In alternative embodiments, BLAST, BLAST 2.0 and BLAST 2.2.2 algorithmsare used to practice the invention. They are described, e.g., inAltschul (1977) Nuc. Acids Res. 25:3389-3402; Altschul (1990) J. Mol.Biol. 215:403-410. Software for performing BLAST analyses is publiclyavailable through the National Center for Biotechnology Information.This algorithm involves first identifying high scoring sequence pairs(HSPs) by identifying short words of length W in the query sequence,which either match or satisfy some positive-valued threshold score Twhen aligned with a word of the same length in a database sequence. T isreferred to as the neighborhood word score threshold (Altschul (1990)supra). These initial neighborhood word hits act as seeds for initiatingsearches to find longer HSPs containing them. The word hits are extendedin both directions along each sequence for as far as the cumulativealignment score can be increased. Cumulative scores are calculatedusing, for nucleotide sequences, the parameters M (reward score for apair of matching residues; always >0). For amino acid sequences, ascoring matrix is used to calculate the cumulative score. Extension ofthe word hits in each direction are halted when: the cumulativealignment score falls off by the quantity X from its maximum achievedvalue; the cumulative score goes to zero or below, due to theaccumulation of one or more negative-scoring residue alignments; or theend of either sequence is reached. The BLAST algorithm parameters W, T,and X determine the sensitivity and speed of the alignment. The BLASTNprogram (for nucleotide sequences) uses as defaults a wordlength (W) of11, an expectation (E) of 10, M=5, N=−4 and a comparison of bothstrands. For amino acid sequences, the BLASTP program uses as defaults awordlength of 3, and expectations (E) of 10, and the BLOSUM62 scoringmatrix (see Henikoff & Henikoff (1989) Proc. Natl. Acad. Sci. USA89:10915) alignments (B) of 50, expectation (E) of 10, M=5, N=−4, and acomparison of both strands. The BLAST algorithm also performs astatistical analysis of the similarity between two sequences (see, e.g.,Karlin & Altschul (1993) Proc. Natl. Acad. Sci. USA 90:5873). Onemeasure of similarity provided by BLAST algorithm is the smallest sumprobability (P(N)), which provides an indication of the probability bywhich a match between two nucleotide or amino acid sequences would occurby chance. For example, a nucleic acid is considered similar to areferences sequence if the smallest sum probability in a comparison ofthe test nucleic acid to the reference nucleic acid is less than about0.2, less than about 0.01, or less than about 0.001. In one aspect,protein and nucleic acid sequence homologies are evaluated using theBasic Local Alignment Search Tool (“BLAST”). For example, five specificBLAST programs can be used to perform the following task: (1) BLASTP andBLAST3 compare an amino acid query sequence against a protein sequencedatabase; (2) BLASTN compares a nucleotide query sequence against anucleotide sequence database; (3) BLASTX compares the six-frameconceptual translation products of a query nucleotide sequence (bothstrands) against a protein sequence database; (4) TBLASTN compares aquery protein sequence against a nucleotide sequence database translatedin all six reading frames (both strands); and, (5) TBLASTX compares thesix-frame translations of a nucleotide query sequence against thesix-frame translations of a nucleotide sequence database. The BLASTprograms identify homologous sequences by identifying similar segments,which are referred to herein as “high-scoring segment pairs,” between aquery amino or nucleic acid sequence and a test sequence which can beobtained from a protein or nucleic acid sequence database. High-scoringsegment pairs can be identified (i.e., aligned) by means of a scoringmatrix, many of which are known in the art. An exemplary scoring matrixused is the BLOSUM62 matrix (Gonnet et al., Science 256:1443-1445, 1992;Henikoff and Henikoff, Proteins 17:49-61, 1993). Alternatively, the PAMor PAM250 matrices may be used (see, e.g., Schwartz and Dayhoff, eds.,1978, Matrices for Detecting Distance Relationships: Atlas of ProteinSequence and Structure, Washington: National Biomedical ResearchFoundation).

In one aspect of the invention, to determine if a nucleic acid has therequisite sequence identity to be within the scope of the invention, theNCBI BLAST 2.2.2 programs is used. default options to blastp. There areabout 38 setting options in the BLAST 2.2.2 program. In this exemplaryaspect of the invention, all default values are used except for thedefault filtering setting (i.e., all parameters set to default exceptfiltering which is set to OFF); in its place a “—F F” setting is used,which disables filtering. Use of default filtering often results inKarlin-Altschul violations due to short length of sequence.

The default values used in this exemplary aspect of the inventioninclude:

“Filter for low complexity: ON

-   -   >Word Size: 3    -   >Matrix: Blosum62    -   >Gap Costs: Existence:11        -   >Extension:1”

“Filter for low complexity: ON

Other default settings are: filter for low complexity OFF, word size of3 for protein, BLOSUM62 matrix, gap existence penalty of −11 and a gapextension penalty of −1.

6.7. Inhibiting Expression of a Polypeptide

The invention further provides for nucleic acids complementary(partially or completely complementary) to (e.g., antisense sequencesto) the nucleic acid sequences of the invention, including nucleic acidscomprising e.g., antisense, iRNA, miRNA, ribozymes. Antisense sequencesare capable of inhibiting the transport, splicing or transcription ofpolypeptide-encoding genes. The inhibition can be effected through thetargeting of genomic DNA or messenger RNA. The transcription or functionof targeted nucleic acid can be inhibited, for example, by hybridizationand/or cleavage. One particularly useful set of inhibitors provided bythe present invention includes oligonucleotides which are able to eitherbind polypeptide-encoding genes or messages, in either case preventingor inhibiting the production or function of the polypeptide. Theassociation can be though sequence specific hybridization. Anotheruseful class of inhibitors includes oligonucleotides which causeinactivation or cleavage of the polypeptide message. The oligonucleotidecan have enzyme activity which causes such cleavage, such as ribozymes.The oligonucleotide can be chemically modified or conjugated to anenzyme or composition capable of cleaving the complementary nucleicacid. One may screen a pool of many different such oligonucleotides forthose with the desired activity.

6.8. Antisense Oligonucleotides

The invention provides antisense oligonucleotides capable of bindingmessages and/or genes of nucleic acids of the invention; which inalternative embodiments can inhibit polypeptide activity by targetinggene or mRNA. Strategies for designing antisense oligonucleotides arewell described in the scientific and patent literature, and the skilledartisan can design such oligonucleotides using the novel reagents of theinvention. For example, gene walking/RNA mapping protocols to screen foreffective antisense oligonucleotides are well known in the art, see,e.g., Ho (2000) Methods Enzymol. 314:168-183, describing an RNA mappingassay, which is based on standard molecular techniques to provide aneasy and reliable method for potent antisense sequence selection. Seealso Smith (2000) Euro. J. Pharm. Sci. 11:191-198.

Naturally occurring nucleic acids are used as antisenseoligonucleotides. The antisense oligonucleotides can be of any length;for example, in alternative aspects, the antisense oligonucleotides arebetween about 5 to 100, about 10 to 80, about 15 to 60, about 18 to 40.The optimal length can be determined by routine screening. The antisenseoligonucleotides can be present at any concentration. The optimalconcentration can be determined by routine screening. A wide variety ofsynthetic, non-naturally occurring nucleotide and nucleic acid analoguesare known which can address this potential problem. For example, peptidenucleic acids (PNAs) containing non-ionic backbones, such asN-(2-aminoethyl) glycine units can be used. Antisense oligonucleotideshaving phosphorothioate linkages can also be used, as described in WO97/03211; WO 96/39154; Mata (1997) Toxicol Appl Pharmacol 144:189-197;Antisense Therapeutics, ed. Agarwal (Humana Press, Totowa, N.J., 1996).Antisense oligonucleotides having synthetic DNA backbone analoguesprovided by the invention can also include phosphoro-dithioate,methylphosphonate, phosphoramidate, alkyl phosphotriester, sulfamate,3′-thioacetal, methylene(methylimino), 3′-N-carbamate, and morpholinocarbamate nucleic acids, as described above.

Combinatorial chemistry methodology can be used to create vast numbersof oligonucleotides that can be rapidly screened for specificoligonucleotides that have appropriate binding affinities andspecificities toward any target, such as the sense and antisense ENZYMEsequences of the invention (see, e.g., Gold (1995) J. of Biol. Chem.270:13581-13584).

6.9. Inhibitory Ribozymes

The invention provides ribozymes comprising nucleic acid sequences ofthe invention, where in alternative embodiments the ribozymes of theinvention are capable of binding messages or genes which can inhibitenzyme activity or expression by targeting mRNA or genes. Strategies fordesigning ribozymes and selecting the polypeptide-specific antisensesequence for targeting are well described in the scientific and patentliterature, and the skilled artisan can design such ribozymes using thenovel reagents of the invention. Ribozymes act by binding to a targetRNA through the target RNA binding portion of a ribozyme which is heldin close proximity to an enzymatic portion of the RNA that cleaves thetarget RNA. Thus, the ribozyme recognizes and binds a target RNA throughcomplementary base-pairing, and once bound to the correct site, actsenzymatically to cleave and inactivate the target RNA. Cleavage of atarget RNA in such a manner will destroy its ability to direct synthesisof an encoded protein if the cleavage occurs in the coding sequence.After a ribozyme has bound and cleaved its RNA target, it is typicallyreleased from that RNA and so can bind and cleave new targetsrepeatedly.

In some circumstances, the enzymatic nature of a ribozyme can beadvantageous over other technologies, such as antisense technology(where a nucleic acid molecule simply binds to a nucleic acid target toblock its transcription, translation or association with anothermolecule) as the effective concentration of ribozyme necessary to effecta therapeutic treatment can be lower than that of an antisenseoligonucleotide. This potential advantage reflects the ability of theribozyme to act enzymatically. Thus, a single ribozyme molecule is ableto cleave many molecules of target RNA. In addition, a ribozyme istypically a highly specific inhibitor, with the specificity ofinhibition depending not only on the base pairing mechanism of binding,but also on the mechanism by which the molecule inhibits the expressionof the RNA to which it binds. That is, the inhibition is caused bycleavage of the RNA target and so specificity is defined as the ratio ofthe rate of cleavage of the targeted RNA over the rate of cleavage ofnon-targeted RNA. This cleavage mechanism is dependent upon factorsadditional to those involved in base pairing. Thus, the specificity ofaction of a ribozyme can be greater than that of antisenseoligonucleotide binding the same RNA site. The enzymatic ribozyme RNAmolecule can be formed in a hammerhead motif, but may also be formed inthe motif of a hairpin, hepatitis delta virus, group I intron orRNaseP-like RNA (in association with an RNA guide sequence). Examples ofsuch hammerhead motifs are described by Rossi (1992) Aids Research andHuman Retroviruses 8:183; hairpin motifs by Hampel (1989) Biochemistry28:4929, and Hampel (1990) Nuc. Acids Res. 18:299; the hepatitis deltavirus motif by Perrotta (1992) Biochemistry 31:16; the RNaseP motif byGuerrier-Takada (1983) Cell 35:849; and the group I intron by Cech U.S.Pat. No. 4,987,071. The recitation of these specific motifs is notintended to be limiting; those skilled in the art will recognize that anenzymatic RNA molecule of this invention has a specific substratebinding site complementary to one or more of the target gene RNAregions, and has nucleotide sequence within or surrounding thatsubstrate binding site which imparts an RNA cleaving activity to themolecule.

6.10. RNA Interference (RNAi)

In one aspect, the invention provides an RNA inhibitory molecule, aso-called “RNAi” molecule, comprising an enzyme sequence of theinvention. The RNAi molecule comprises a double-stranded RNA (dsRNA)molecule. The RNAi molecule, e.g., siRNA and/or miRNA, can inhibitexpression of a nucleic acid of the invention, e.g., a message or agene. In one aspect, the RNAi molecule, e.g., siRNA and/or miRNA, isabout 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25 or more duplexnucleotides in length.

While the invention is not limited by any particular mechanism ofaction, the RNAi, e.g., siRNA and/or miRNA, can enter a cell and causethe degradation of a single-stranded RNA (ssRNA) of similar or identicalsequences, including endogenous mRNAs. When a cell is exposed todouble-stranded RNA (dsRNA), mRNA from the homologous gene isselectively degraded by a process called RNA interference (RNAi). Apossible basic mechanism behind RNAi is the breaking of adouble-stranded RNA (dsRNA) matching a specific gene sequence into shortpieces called short interfering RNA, which trigger the degradation ofmRNA that matches its sequence. In one aspect, the RNAi's of theinvention are used in gene-silencing therapeutics, see, e.g., Shuey(2002) Drug Discov. Today 7:1040-1046. In one aspect, the inventionprovides methods to selectively degrade RNA using the RNAi's molecules,e.g., siRNA and/or miRNA, of the invention. In one aspect, themicro-inhibitory RNA (miRNA) inhibits translation, and the siRNAinhibits transcription. The process may be practiced in vitro, ex vivoor in vivo. In one aspect, the RNAi molecules of the invention can beused to generate a loss-of-function mutation in a cell, an organ or ananimal Methods for making and using RNAi molecules, e.g., siRNA and/ormiRNA, for selectively degrade RNA are well known in the art, see, e.g.,U.S. Pat. Nos. 6,506,559; 6,511,824; 6,515,109; 6,489,127.

6.11. Modification of Nucleic Acids

The invention provides methods of generating variants of the nucleicacids of the invention, e.g., those encoding a cellulase or acellobiohydrolase (cbhl) enzyme. These methods can be repeated or usedin various combinations to generate cellulase or cellobiohydrolase(cbhl) enzymes having an altered or different activity or an altered ordifferent stability from that of a polypeptide encoded by the templatenucleic acid. These methods also can be repeated or used in variouscombinations, e.g., to generate variations in gene/message expression,message translation or message stability. In another aspect, the geneticcomposition of a cell is altered by, e.g., modification of a homologousgene ex vivo, followed by its reinsertion into the cell.

The invention also provides methods for changing the characteristics ofa polypeptide of the invention by mutagenesis and other method,including directed evolution, e.g., DirectEvolution® technology; (see,e.g., U.S. Pat. No. 5,830,696; Gene Site Saturation Mutagenesis^(SM)(GSSM^(SM)) technology (see, e.g., U.S. Pat. Nos. 6,171,820 and6,579,258), Exonuclease-Mediated Gene Assembly in Directed Evolution(see, e.g., U.S. Pat. Nos. 6,361,974 and 6,352,842), End Selection inDirected Evolution (see, e.g., U.S. Pat. Nos. 6,358,709 and 6,238,884),Recombination-Based Synthesis Shuffling (see, e.g., U.S. Pat. Nos.5,965,408 and 6,440,668, and Australian Patent No. AU724521), andDirected Evolution of Thermophilic Enzymes (see, e.g., U.S. Pat. Nos.5,830,696 and 6,335,179).

A nucleic acid of the invention can be altered by any means. Forexample, random or stochastic methods, or, non-stochastic, or “directedevolution,” methods. Methods for random mutation of genes are well knownin the art, see, e.g., U.S. Pat. No. 5,830,696.

Alternatively, nucleic acids, e.g., genes, can be reassembled afterrandom, or “stochastic,” fragmentation, see, e.g., U.S. Pat. Nos.6,291,242; 6,287,862; 6,287,861; 5,955,358; 5,830,721; 5,824,514;5,811,238; 5,605,793. In alternative aspects, modifications, additionsor deletions are introduced by error-prone PCR, shuffling,oligonucleotide-directed mutagenesis, assembly PCR, sexual PCRmutagenesis, in vivo mutagenesis, cassette mutagenesis, recursiveensemble mutagenesis, exponential ensemble mutagenesis, site-specificmutagenesis, GeneReassembly, Gene Site Saturation Mutagenesis (GSSM),Tailored Multi-Site Combinatorial Assembly, recursive sequencerecombination, phosphothioate-modified DNA mutagenesis,uracil-containing template mutagenesis, gapped duplex mutagenesis, pointmismatch repair mutagenesis, repair-deficient host strain mutagenesis,chemical mutagenesis, radiogenic mutagenesis, deletion mutagenesis,restriction-selection mutagenesis, restriction-purification mutagenesis,artificial gene synthesis, ensemble mutagenesis, chimeric nucleic acidmultimer creation, and/or a combination of these and other methods.

In alternative embodiments, a non-stochastic gene modification systemsuch as “GeneReassembly” technology or a “directed evolution process,”is used to generate polypeptides, e.g., enzymes or antibodies of theinvention, with new or altered properties. GeneRessembly technology is amethod of ligating oligonucleotide segments together non-stochastically.This method differs from stochastic oligonucleotide shuffling in thatthe nucleic acid building blocks are not shuffled, concatenated orchimerized randomly, but rather are assembled non-stochastically. See,e.g., U.S. Pat. Nos. 6,773,900; 6,740,506; 6,713,282; 6,635,449;6,605,449; 6,537,776.

In alternative embodiments, Tailored Multi-Site Combinatorial Assembly(TMCA) technology, TMCA technology (see PCT Publication No. WO09/018,449), is used to produce a plurality of progeny polynucleotideshaving different combinations of various mutations at multiple sites.

6.12. Transgenic Plants and Seeds

The invention provides transgenic plants and seeds comprising a nucleicacid, a polypeptide, an expression cassette, cloning mechanism or vectorof the invention, or a transfected or transformed cell of the invention.The invention also provides plant products, e.g., oils, seeds, leaves,extracts and the like, comprising a nucleic acid and/or a polypeptide ofthe invention. The transgenic plant can be dicotyledonous (a dicot) ormonocotyledonous (a monocot). The invention also provides methods ofmaking and using these transgenic plants and seeds. The transgenic plantor plant cell expressing a polypeptide of the present invention may beconstructed in accordance with any method known in the art. See, forexample, U.S. Pat. No. 6,309,872.

The recombinant expression, or over-expression, of the sequences of theinvention may be achieved in combination with one or more additionalmolecules such as, for example, other enzymes. This approach is usefulfor producing combination products, such as a plant or plant part thatcontains sequences of the invention as well as one or more additionalmolecules. The molecules of this invention and the additional moleculescan be used in a combination treatment. The resulting recombinantlyexpressed molecules may be used in homogenized and/or purified form oralternatively in relatively unpurified form (e.g. as consumable plantparts that are useful when admixed with other foodstuffs for catalyzingthe degradation of phytate).

In a particular aspect, the present invention provides for theexpression of sequences of the invention in transgenic plants or plantorgans and methods for the production thereof. DNA expression constructsare provided for the transformation of plants with a gene encodingsequences of the invention under the control of regulatory sequenceswhich are capable of directing the expression of sequences of theinvention. These regulatory sequences include sequences capable ofdirecting transcription in plants, either constitutively, or in stageand/or tissue specific manners.

The manner of expression depends, in part, on the use of the plant orparts thereof. The transgenic plants and plant organs provided by thepresent invention may be applied to a variety of industrial processeseither directly, e.g. in animal feeds or alternatively, the expressedpolypeptide of the invention may be extracted and if desired, purifiedbefore application. Alternatively, the recombinant host plant or plantpart may be used directly. In a particular aspect, the present inventionprovides methods of catalyzing phytate-hydrolyzing reactions using seedscontaining enhanced amounts of polypeptide. The method involvescontacting transgenic, non-wild type seeds, e.g., in a ground or chewedform, with phytate-containing substrate and allowing the enzymes in theseeds to increase the rate of reaction. By directly adding the seeds toa phytate-containing substrate, the invention provides a solution to theexpensive and problematic process of extracting and purifying theenzyme. In one exemplification the present invention provides methods oftreatment whereby an organism lacking a sufficient supply of an enzymeis administered the enzyme in the form of seeds containing enhancedamounts of the enzyme. In one aspect, the timing of the administrationof the enzyme to an organism is coordinated with the consumption of aphytate-containing foodstuff.

The expression of polypeptides and nucleic acides of the invention inplants can be achieved by a variety of means. Specifically, for example,technologies are available for transforming a large number of plantspecies, including dicotyledonous species (e.g. tobacco, potato, tomato,Petunia, Brassica) and monocot species. Additionally, for example,strategies for the expression of foreign genes in plants are available.Additionally still, regulatory sequences from plant genes have beenidentified that are serviceable for the construction of chimeric genesthat can be functionally expressed in plants and in plant cells (e.g.Klee (1987) Ann. Rev. of Plant Phys. 38:467-486; Clark et al. (1990)Virology December; 179(2):640-7; Smith et al. (1990) Mol. Gen. Genet.December; 224(3):477-81.

The introduction of gene constructs into plants can be achieved usingseveral technologies including transformation with Agrobacteriumtumefaciens or Agrobacterium rhizogenes. Non-limiting examples of planttissues that can be transformed thusly include protoplasts, microsporesor pollen, and explants such as leaves, stems, roots, hypocotyls, andcotyls. Furthermore, DNA can be introduced directly into protoplasts andplant cells or tissues by microinjection, electroporation, particlebombardment, and direct DNA uptake.

Proteins may be produced in plants by a variety of expression systems.For instance, the use of a constitutive promoter such as the 35Spromoter of Cauliflower Mosaic Virus (Guilley et al., 1982) isserviceable for the accumulation of the expressed protein in virtuallyall organs of the transgenic plant. Alternatively, the use of promotersthat are highly tissue-specific and/or stage-specific are serviceablefor this invention (Higgins, 1984; Shotwell, 1989) in order to biasexpression towards desired tissues and/or towards a desired stage ofdevelopment. The invention also uses protocols for expression in plantsof ENZYME molecules of the instant invention as disclosed in, forexample, U.S. Pat. No. 5,770,413 (Van Ooijen et al.) and U.S. Pat. No.5,593,963 (Van Ooijen et al.), that teaches use of fungal enzymes.

6.13. Modification of Coding Sequences and Adjacent Sequences

In alternative embodiments, the invention provides transgenic expressionin plants and plant cells of nucleic acids (e.g., genes) of theinvention, and modification of those nucleic acids and genes of theinvention to achieve and optimize their expression in host expressionplants and plant cells. In alternative embodiments, bacterial ORFs whichencode separate enzymes but which are encoded by the same transcript inthe native microbe are used for expression in plants on separatetranscripts. In alternative embodiments, to achieve this, each microbialORF is isolated individually and cloned within a cassette which providesa plant promoter sequence at the 5′ end of the ORF and a planttranscriptional terminator at the 3′ end of the ORF. The isolated ORFsequence can includes the initiating ATG codon and the terminating STOPcodon but may include additional sequence beyond the initiating ATG andthe STOP codon. In addition, the ORF may be truncated, but still retainthe required activity; for particularly long ORFs, truncated versionswhich retain activity may be preferable for expression in transgenicorganisms. “Plant promoters” and “plant transcriptional terminators”that can be used to practice this invention include any promoters and/ortranscriptional terminators which operate within plant cells. Thisincludes promoters and transcription terminators which may be derivedfrom non-plant sources such as viruses (e.g., a Cauliflower MosaicVirus).

In alternative embodiments, modification to the ORF coding sequences andadjacent sequence is not required. It is sufficient to isolate afragment containing the ORF of interest and to insert it downstream of aplant promoter. For example, Gaffney et. al. (Science 261: 754-756(1993)) have expressed the Pseudomonas nahG gene in transgenic plantsunder the control of the CaMV 35S promoter and the CaMV tml terminatorsuccessfully without modification of the coding sequence and withnucleotides of the Pseudomonas gene upstream of the ATG still attached,and nucleotides downstream of the STOP codon still attached to the nahGORF. Preferably as little adjacent microbial sequence should be leftattached upstream of the ATG and downstream of the STOP codon. Inpractice, such construction may depend on the availability ofrestriction sites.

In alternative embodiments, expression of genes derived from microbialsources may provide problems in expression. These problems have beenwell characterized in the art and are particularly common with genesinitially derived from certain microbial sources. These problems mayapply to the nucleotide sequence of this invention and the modificationof these genes can be undertaken using techniques now well known in theart. The following problems may be encountered:

6.14. Codon Usage

In alternative embodiments, the invention provides nucleic acids havingcodons modified for usage in plants; in some cases preferred codon usagein plants differs from the preferred codon usage in certainmicroorganisms. Comparison of the usage of codons within a clonedmicrobial ORF to usage in plant genes (and in particular genes from thetarget plant) will enable an identification of the codons within the ORFwhich should preferably be changed. Typically plant evolution has tendedtowards a strong preference of the nucleotides C and G in the third baseposition of monocotyledons, whereas dicotyledons often use thenucleotides A or T at this position. By modifying a gene to incorporatepreferred codon usage for a particular target transgenic species, manyof the problems described below for GC/AT content and illegitimatesplicing will be overcome.

6.15. GC/AT Content

In alternative embodiments, the invention provides nucleic acids havingtheir GC content modified, e.g., for usage in plants; plant genestypically have a GC content of more than 35%. ORF sequences which arerich in A and T nucleotides can cause several problems in plants.Firstly, motifs of ATTTA are believed to cause destabilization ofmessages and are found at the 3′ end of many short-lived mRNAs.Secondly, the occurrence of polyadenylation signals such as AATAAA atinappropriate positions within the message is believed to causepremature truncation of transcription. In addition, monocotyledons mayrecognize AT-rich sequences as splice sites (see below).

Sequences Adjacent to the Initiating Methionine

In alternative embodiments, the invention provides nucleic acids havingnucleotides adjacent to the ATG modified and/or added; plants differfrom microorganisms in that their messages do not possess a definedribosome binding site. Rather, it is believed that ribosomes attach tothe 5′ end of the message and scan for the first available ATG at whichto start translation. Nevertheless, it is believed that there is apreference for certain nucleotides adjacent to the ATG and thatexpression of microbial genes can be enhanced by the inclusion of aeukaryotic consensus translation initiator at the ATG. Clontech(1993/1994 catalog, page 210, incorporated herein by reference) havesuggested one sequence as a consensus translation initiator for theexpression of the E. coli uidA gene in plants. Further, Joshi (N.A.R.15: 6643-6653 (1987), incorporated herein by reference) has comparedmany plant sequences adjacent to the ATG and suggests another consensussequence. In situations where difficulties are encountered in theexpression of microbial ORFs in plants, inclusion of one of thesesequences at the initiating ATG may improve translation. In such casesthe last three nucleotides of the consensus may not be appropriate forinclusion in the modified sequence due to their modification of thesecond AA residue. In some aspects, preferred sequences adjacent to theinitiating methionine may differ between different plant species. Asurvey of 14 maize genes located in the GenBank database provided thefollowing results:

Position Before the Initiating ATG in 14 Maize Genes

−10 −9 −8 −7 −6 −5 −4 −3 −2 −1 C 3 8 4 6 2 5 6 0 10 7 T 3 0 3 4 3 2 1 11 0 A 2 3 1 4 3 2 3 7 2 3 G 6 3 6 0 6 5 4 6 1 5

This analysis can be done for the desired plant species into which thenucleotide sequence is being incorporated, and the sequence adjacent tothe ATG modified to incorporate the preferred nucleotides.

6.16. Removal of Illegitimate Splice Sites

In alternative embodiments, the invention provides nucleic acids havingillegitimate splice sites modified or removed or functionally “knockedout”; genes cloned from non-plant sources and not optimized forexpression in plants may also contain motifs which may be recognized inplants as 5′ or 3′ splice sites, and be cleaved, thus generatingtruncated or deleted messages. These sites can be removed using thetechniques well known in the art.

Techniques for the modification of coding sequences and adjacentsequences are well known in the art. In cases where the initialexpression of a microbial ORF is low and it is deemed appropriate tomake alterations to the sequence as described above, then theconstruction of synthetic genes can be accomplished according to methodswell known in the art. These are, for example, described in thepublished patent disclosures EP 0 385 962 (to Monsanto), EP 0 359 472(to Lubrizol) and WO 93/07278 (to Ciba-Geigy), all of which areincorporated herein by reference. In most cases it is preferable toassay the expression of gene constructions using transient assayprotocols (which are well known in the art) prior to their transfer totransgenic plants.

6.17. Plant Promoters and Transcriptional Control Motifs

In alternative embodiments, nucleic acids of the invention comprisetranscriptional control motifs, e.g., promoters, e.g., fortransformation and expression in a plant of interest. The nucleic acidsequences may be present in DNA constructs or expression cassettes.Nucleic acids of the invention can be, or comprise, “expressioncassettes”, including any nucleic acid molecule capable of directingexpression of a particular nucleotide sequence in an appropriate hostcell comprising a promoter operatively linked to the nucleotide sequenceof interest which is operatively linked to termination signals.

The compositions (e.g., nucleic acid sequences) of the invention alsocan comprise sequences required for proper translation of the nucleotidesequence. The coding region usually codes for a protein of interest butmay also code for a functional RNA of interest, for example antisenseRNA or a nontranslated RNA, in the sense or antisense direction. Theexpression cassette comprising the nucleotide sequence of interest maybe chimeric, meaning that at least one of its components is heterologouswith respect to at least one of its other components. The expressioncassette may also be one that is naturally occurring but has beenobtained in a recombinant form useful for heterologous expression.Typically, however, the expression cassette is heterologous with respectto the host, i.e., the particular DNA sequence of the expressioncassette does not occur naturally in the host cell and must have beenintroduced into the host cell or an ancestor of the host cell by atransformation event. The expression of the nucleotide sequence in theexpression cassette may be under the control of a constitutive promoteror of an inducible promoter that initiates transcription only when thehost cell is exposed to some particular external stimulus. Additionally,the promoter can also be specific to a particular tissue or organ orstage of development.

In alternative embodiments the invention provides for the transformationof plants with expression cassettes capable of expressingpolynucleotides of the invention. The expression cassette will includein the 5′-3′ direction of transcription, a transcriptional andtranslational initiation region (i.e., a promoter) and a polynucleotideof interest. The expression cassette may optionally comprise atranscriptional and translational termination region (i.e. terminationregion) functional in plants. In some embodiments, the expressioncassette comprises a selectable marker gene to allow for selection forstable transformants. Expression constructs of the invention may alsocomprise a leader sequence and/or a sequence allowing for inducibleexpression of the polynucleotide of interest. See, Guo et. al. (2003)Plant J. 34:383-92 and Chen et. al. (2003) Plant J. 36:731-40 forexamples of sequences allowing for inducible expression.

In alternative embodiments regulatory sequences of the expressionconstruct are operably linked to the polynucleotide of interest. By“operably linked” is intended a functional linkage between a promoterand a second sequence wherein the promoter sequence initiates andmediates transcription of the DNA sequence corresponding to the secondsequence. In alternative embodiments, operably linked means that thenucleotide sequences being linked are contiguous.

Any promoter capable of driving expression in the plant of interest maybe used in the practice of the invention. The promoter may be native oranalogous or foreign or heterologous to the plant host. The terms“heterologous” and “exogenous” when used herein to refer to a nucleicacid sequence (e.g. a DNA or RNA sequence) or a gene, refer to asequence that originates from a source foreign to the particular hostcell or, if from the same source, is modified from its original form.Thus, a heterologous gene in a host cell includes a gene that isendogenous to the particular host cell but has been modified. The termsalso include non-naturally occurring multiple copies of a naturallyoccurring DNA sequence. Thus, the terms refer to a DNA segment that isforeign or heterologous to the cell, or homologous to the cell but in aposition within the host cell nucleic acid in which the element is notordinarily found. Exogenous DNA segments are expressed to yieldexogenous polypeptides. In alternative embodiments, a “homologous”nucleic acid (e.g. DNA) sequence is a nucleic acid (e.g. DNA or RNA)sequence naturally associated with a host cell into which it isintroduced.

The choice of promoters to be included depends upon several factors,including, but not limited to, efficiency, selectability, inducibility,desired expression level, and cell- or tissue-preferential expression.It is a routine matter for one of skill in the art to modulate theexpression of a sequence by appropriately selecting and positioningpromoters and other regulatory regions relative to that sequence.

Some suitable promoters initiate transcription only, or predominantly,in certain cell types. Thus, as used herein a cell type- ortissue-preferential promoter is one that drives expressionpreferentially in the target tissue, but may also lead to someexpression in other cell types or tissues as well. Methods foridentifying and characterizing promoter regions in plant genomic DNAinclude, for example, those described in the following references:Jordano, et. al., Plant Cell, 1:855-866 (1989); Bustos, et. al., PlantCell, 1:839-854 (1989); Green, et. al., EMBO J. 7, 4035-4044 (1988);Meier, et. al., Plant Cell, 3, 309-316 (1991); and Zhang, et. al., PlantPhysiology 110: 1069-1079 (1996).

In alternative embodiments tissue-preferred regulated genes and/orpromoters for plants or specific tissues, organs and/or cells are used.Some reported tissue preferred genes include the genes encoding the seedstorage proteins (such as napin, cruciferin, beta-conglycinin, andphaseolin, prolamines, glutelins, globulins, and zeins) zeins or oilbody proteins (such as oleosin), or genes involved in fatty acidbiosynthesis (including acyl carrier protein, stearoyl-ACP desaturase,and fatty acid desaturases (fad 2-1)), and other genes expressed duringembryo development (such as Bce4, see, for example, EP 255378 and Kridlet. al., (1991) Seed Science Research, 1:209).

Examples of tissue-specific promoters which can be used to practice thisinvention include the lectin (Vodkin, Prog. Clin. Biol. Res., 138; 87(1983); Lindstrom et. al., (1990) Der. Genet., 11:160), corn alcoholdehydrogenase 1 (Dennis et. al., Nucleic Acids Res., 12:3983 (1984)),corn light harvesting complex (see, e.g., Simpson, (1986) Science,233:34; Bansal (1992) Proc. Natl. Acad. Sci. USA 89:3654), corn heatshock protein (see, e.g., Odell et. al., (1985) Nature, 313:810; peasmall subunit RuBP carboxylase (see, e.g., Poulsen et. al., (1986) Mol.Gen. Genet., 205:193-200; Cashmore et. al., (1983) Gen. Eng. of Plants,Plenum Press, New York, 29-38); Ti plasmid mannopine synthase (see,e.g., Langridge et. al., (1989) Proc. Natl. Acad. Sci. USA,86:3219-3223), Ti plasmid nopaline synthase (Langridge et. al., (1989)Proc. Natl. Acad. Sci. USA, 86:3219-3223), petunia chalcone isomerase(see, e.g., vanTunen (1988) EMBO J. 7:1257); bean glycine rich protein 1(see, e.g., Keller (1989) Genes Dev. 3:1639); truncated CaMV 35S (see,e.g., Odell (1985) Nature 313:810); potato patatin (see, e.g., Wenzler(1989) Plant Mol. Biol. 13:347; root cell (see, e.g., Yamamoto (1990)Nucleic Acids Res. 18:7449); maize zein (see, e.g., Reina (1990) NucleicAcids Res. 18:6425; Lopes et. al. (1995) Mol. Gen. Genet. 247: 603-613;Kriz (1987) Mol. Gen. Genet. 207:90; Wandelt (1989) Nucleic Acids Res.,17:2354; Langridge (1983) Cell, 34:1015; Reina (1990) Nucleic AcidsRes., 18:7449), ADP-gpp promoter (see, e.g., U.S. Pat. No. 7,102,057);globulin-1 (see, e.g., Belanger (1991) Genetics 129:863); α-globulin(Sunilkumar, et. al. (2002), Transgenic Res. 11:347-359); □-tubulin; cab(see, e.g., Sullivan (1989) Mol. Gen. Genet., 215:431); PEPCase (seee.g., Hudspeth & Grula, (1989) Plant Molec. Biol., 12:579-589); R genecomplex-associated promoters (Chandler et. al., (1989) Plant Cell,1:1175); pea vicilin promoter (Czako et. al., (1992) Mol. Gen. Genet.,235:33; U.S. Pat. No. 5,625,136); GTL1 promoter (Takaiwa et. al. (1991)Plant Mol. Biol. 16 (1), 49-58); chalcone synthase promoters (Frankenet. al., (1991) EMBO J., 10:2605); GY1 promoter (Sims & Goldburg (1989)Nuc. Acid Res. 17(11) 4368) and the like; all of which are hereinincorporated by reference.

In alternative embodiments the invention uses fruit-preferred promoters,including any class of fruit-preferred promoters, e.g., as expressed ator during antithesis through fruit development, at least until thebeginning of ripening, e.g., as discussed in U.S. Pat. No. 4,943,674,the disclosure of which is hereby incorporated by reference. Thepromoter for polygalacturonase gene is active in fruit ripening. Theinvention can use the polygalacturonase gene as described, e.g., in U.S.Pat. No. 4,535,060, U.S. Pat. No. 4,769,061, U.S. Pat. No. 4,801,590,and U.S. Pat. No. 5,107,065, which disclosures are incorporated hereinby reference.

In alternative embodiments the invention uses any tissue-preferredpromoter or transcriptional control element, including e.g., those thatdirect expression in leaf cells following damage to the leaf (forexample, from chewing insects), in tubers (for example, patatin genepromoter), and in fiber cells (an example of a developmentally-regulatedfiber cell protein is E6 (John & Crow (1992) PNAS 89:5769-5773). The E6gene is most active in fiber, although low levels of transcripts arefound in leaf, ovule and flower.

In alternative embodiments the invention uses promoters active inphotosynthetic tissue, e.g., in order to drive transcription in greentissues such as leaves and stems, are suitable when they driveexpression only or predominantly in such tissues. Alternatively, theinvention can use promoters to confer expression constitutivelythroughout the plant, or differentially with respect to the greentissues, or differentially with respect to the developmental stage ofthe green tissue in which expression occurs, or in response to externalstimuli.

Exemplary promoters used to practice this invention include theribulose-1,5-bisphosphate carboxylase (RbcS) promoters such as the RbcSpromoter from eastern larch (Larix laricina), the pine cab6 promoter(Yamamoto et. al. (1994) Plant Cell Physiol. 35:773-778), the Cab-1 genepromoter from wheat (Fejes et. al. (1990) Plant Mol. Biol. 15:921-932),the CAB-1 promoter from spinach (Lubberstedt et. al. (1994) PlantPhysiol. 104:997-1006), the cab1R promoter from rice (Luan et. al.(1992) Plant Cell 4:971-981), the pyruvate orthophosphate dikinase(PPDK) promoter from corn (Matsuoka et. al. (1993) Proc Natl Acad SciUSA 90:9586-9590), the tobacco Lhcbl*2 promoter (Cerdan et. al. (1997)Plant Mol. Biol. 33:245-255), the Arabidopsis thaliana SUC2sucrose-H+symporter promoter (Truernit et. al. (1995) Planta196:564-570), and thylakoid membrane protein promoters from spinach(psaD, psaF, psaE, PC, FNR, atpC, atpD, cab, rbcS. Other promoters thatdrive transcription in stems, leafs and green tissue are described inU.S. Patent Publication No. 2007/0006346.

In some embodiments, the tissue specificity of some “tissue preferred”promoters may not be absolute and may be tested reporter genes such asGus or green fluorescent protein, cyan fluorescent protein, yellowfluorescent protein or red fluorescent protein. One can also achievetissue preferred expression with “leaky” expression by a combination ofdifferent tissue-preferred promoters. Other tissue preferred promoterscan be isolated by one skilled in the art (see U.S. Pat. No. 5,589,379).

In alternative embodiments, plant promoters which are inducible uponexposure to plant hormones, such as auxins, are used to express thenucleic acids of the invention. For example, the invention can use theauxin-response elements E1 promoter fragment (AuxREs) in the soybean(Glycine max L.) (Liu (1997) Plant Physiol. 115:397-407); theauxin-responsive Arabidopsis GST6 promoter (also responsive to salicylicacid and hydrogen peroxide) (Chen (1996) Plant J. 10: 955-966); theauxin-inducible parC promoter from tobacco (Sakai (1996) 37:906-913); aplant biotin response element (Streit (1997) Mol. Plant. MicrobeInteract. 10:933-937); and, the promoter responsive to the stresshormone abscisic acid (Sheen (1996) Science 274:1900-1902).

In alternative embodiments the nucleic acids of the invention can alsobe operably linked to plant promoters which are inducible upon exposureto chemicals reagents which can be applied to the plant, such asherbicides or antibiotic. For example, gene expression systems that areactivated in the presence of a chemical ligand, including ethanol, suchas can be found in WO 96/27673; WO 93/01294; WO 94/03619; WO 02/061102,all of which are hereby incorporated by reference. The maize In2-2promoter, activated by benzenesulfonamide herbicide safeners, can beused (De Veylder (1997) Plant Cell Physiol. 38:568-577); application ofdifferent herbicide safeners induces distinct gene expression patterns,including expression in the root, hydathodes, and the shoot apicalmeristem. Coding sequence can be under the control of, e.g., atetracycline-inducible promoter, e.g., as described with transgenictobacco plants containing the Avena sativa L. (oat) argininedecarboxylase gene (Masgrau (1997) Plant J. 11:465-473); estrogen, suchas, the ecdysone receptor (WO 01/52620) or, a salicylic acid-responsiveelement (Stange (1997) Plant J. 11:1315-1324). In alternativeembodiments, chemically- (e.g., hormone- or pesticide-) inducedpromoters, i.e., promoter responsive to a chemical are used, e.g., theycan be applied to a transgenic plant in the field, expression of apolypeptide of the invention can be induced at a particular stage ofdevelopment of the plant.

6.18. Targeting of the Gene Product Within the Cell

Any mechanism for targeting gene products, e.g., in plants, can be usedto practice this invention, and such mechanisms are known to exist inplants and the sequences controlling the functioning of these mechanismshave been characterized in some detail. Sequences have beencharacterized which cause the targeting of gene products to other cellcompartments Amino terminal sequences can be responsible for targeting aprotein of interest to any cell compartment, such as, a vacuole,mitochondrion, peroxisome, protein bodies, endoplasmic reticulum,chloroplast, starch granule, amyloplast, apoplast or cell wall of aplant (e.g. Unger et. al. Plant Molec. Biol. 13: 411-418 (1989); Rogerset. al. (1985) Proc. Natl. Acad. Sci. USA 82: 6512-651; U.S. Pat. No.7,102,057; WO 2005/096704, all of which are hereby incorporated byreference). Optionally, the signal sequence may be an N-terminal signalsequence from waxy, an N-terminal signal sequence from y-zein, a starchbinding domain, a C-terminal starch binding domain, a chloroplasttargeting sequence, which imports the mature protein to the chloroplast(Comai et. al. (1988) J. Biol. Chem. 263: 15104-15109; van den Broeck,et. al. (1985) Nature 313: 358-363; U.S. Pat. No. 5,639,949) or asecretion signal sequence from aleurone cells (Koehler & Ho, Plant Cell2: 769-783 (1990)). Additionally, amino terminal sequences inconjunction with carboxy terminal sequences are responsible for vacuolartargeting of gene products (Shinshi et. al. (1990) Plant Molec. Biol.14: 357-368).

In alternative embodiments, the signal sequence selected should includethe known cleavage site, and the fusion constructed should take intoaccount any amino acids after the cleavage site(s), which are requiredfor cleavage. In some cases this requirement may be fulfilled by theaddition of a small number of amino acids between the cleavage site andthe transgene ATG or, alternatively, replacement of some amino acidswithin the transgene sequence. These construction techniques are wellknown in the art and are equally applicable to any cellular compartment.

In alternative embodiments, the above-described mechanisms for cellulartargeting can be utilized not only in conjunction with their cognatepromoters, but also in conjunction with heterologous promoters so as toeffect a specific cell-targeting goal under the transcriptionalregulation of a promoter that has an expression pattern different tothat of the promoter from which the targeting signal derives.

A variety of means can be used to practice this invention, including anymeans to achieve the recombinant expression of a polypeptide or nucleicacid of the invention in a transgenic plant, seed, organ or any plantpart. Such a transgenic plants and plant parts are serviceable assources of recombinantly expressed polypeptide or nucleic acid of theinvention, which can be added directly to phytate-containing sources.Alternatively, the recombinant plant-expressed polypeptide or nucleicacid of the invention can be extracted away from the plant source and,if desired, purified prior to contacting the polypeptide substrate.

Within the context of the present invention, plants that can be selected(used to practice this invention) include, but are not limited to cropsproducing edible flowers such as cauliflower (Brassica oleracea),artichoke (Cynara scolymus), fruits such as apple (Malus, e.g.domesticus), banana (Musa, e.g. acuminata), berries (such as thecurrant, Ribes, e.g. rubrum), cherries (such as the sweet cherry,Prunus, e.g. avium), cucumber (Cucumis, e.g. sativus), grape (Vitis,e.g. vinifera), lemon (Citrus limon), melon (Cucumis melo), nuts (suchas the walnut, Juglans, e.g. regia; peanut, Arachis hypogeae), orange(Citrus, e.g. maxima), peach (Prunus, e.g. persica), pear (Pyra, e.g.communis), plum (Prunus, e.g. domestica), strawberry (Fragaria, e.g.moschata), tomato (Lycopersicon, e.g. esculentum), leafs, such asalfalfa (Medicago, e.g. sativa), cabbages (e.g. Brassica oleracea),endive (Cichoreum, e.g. endivia), leek (Allium, e.g. porrum), lettuce(Lactuca, e.g. sativa), spinach (Spinacia, e.g. oleraceae), tobacco(Nicotiana, e.g. tabacum), roots, such as arrowroot (Maranta, e.g.arundinacea), beet (Beta, e.g. vulgaris), carrot (Daucus, e.g. carota),cassaya (Manihot, e.g. esculenta), turnip (Brassica, e.g. rapa), radish(Raphanus, e.g. sativus), yam (Dioscorea, e.g. esculenta), sweet potato(Ipomoea batatas) and seeds, such as bean (Phaseolus, e.g. vulgaris),pea (Pisum, e.g. sativum), soybean (Glycin, e.g. max), wheat (Triticum,e.g. aestivum), barley (Hordeum, e.g. vulgare), corn (Zea, e.g. mays),rice (Oryza, e.g. sativa), rapeseed (Brassica napus), millet (PanicumL.), sunflower (Helianthus annus), oats (Avena sativa), tubers, such askohlrabi (Brassica, e.g. oleraceae), potato (Solanum, e.g. tuberosum)and the like.

In alternative embodiments, the nucleic acids and polypeptides of theinvention are expressed in or inserted in any plant or seed. Transgenicplants of the invention can be dicotyledonous or monocotyledonous.Examples of monocot transgenic plants of the invention are grasses, suchas meadow grass (blue grass, Poa), forage grass such as festuca, lolium,temperate grass, such as Agrostis, and cereals, e.g., wheat, oats, rye,barley, rice, sorghum, and maize (corn). Examples of dicot transgenicplants of the invention are tobacco, legumes, such as lupins, potato,sugar beet, pea, bean and soybean, and cruciferous plants (familyBrassicaceae), such as cauliflower, rape seed, and the closely relatedmodel organism Arabidopsis thaliana. Thus, the transgenic plants andseeds of the invention include a broad range of plants, including, butnot limited to, species from the genera Anacardium, Arachis, Asparagus,Atropa, Avena, Brassica, Citrus, Citrullus, Capsicum, Carthamus, Cocos,Coffea, Cucumis, Cucurbita, Daucus, Elaeis, Fragaria, Glycine,Gossypium, Helianthus, Heterocallis, Hordeum, Hyoscyamus, Lactuca,Linum, Lolium, Lupinus, Lycopersicon, Malus, Manihot, Majorana,Medicago, Nicotiana, Olea, Oryza, Panieum, Pannisetum, Persea,Phaseolus, Pistachia, Pisum, Pyrus, Prunus, Raphanus, Ricinus, Secale,Senecio, Sinapis, Solanum, Sorghum, Theobromus, Trigonella, Triticum,Vicia, Vitis, Vigna, and Zea.

In alternative embodiments, the nucleic acids of the invention areexpressed in plants which contain fiber cells, including, e.g., cotton,silk cotton tree (Kapok, Ceiba pentandra), desert willow, creosote bush,winterfat, balsa, ramie, kenaf, hemp, roselle, jute, sisal abaca andflax. In alternative embodiments, the transgenic plants of the inventioncan be members of the genus Gossypium, including members of anyGossypium species, such as G. arboreum;. G. herbaceum, G. barbadense,and G. hirsutum.

Additional plants as well as non-plant expression systems can be used topractice this invention. The choice of the plant species is primarilydetermined by the intended use of the plant or parts thereof and theamenability of the plant species to transformation.

In alternative embodiments, any technique available for the introductionof an expression construct containing a polypeptide-encoding DNAsequence into a targeted cell, organ, tissue or plant can be used.Techniques for transforming a wide variety of higher plant species arewell known and described in the technical and scientific literature.See, e.g., Weising (1988) Ann. Rev. Genet. 22:421-477; U.S. Pat. No.5,750,870. Such techniques also can include but are not limited totransformation of protoplasts using the calcium/polyethylene glycolmethod, electroporation and microinjection or (coated) particlebombardment (Potrykus, 1990). In addition to these so-called direct DNAtransformation methods, transformation systems involving vectors arewidely available, such as viral vectors (e.g. from the CauliflowerMosaic Cirus (CaMV) and bacterial vectors (e.g. from the genusAgrobacterium) (Potrykus, 1990). After selection and/or screening, theprotoplasts, cells or plant parts that have been transformed can beregenerated into whole plants, using methods known in the art (Horsch etal., 1985). The choice of the transformation and/or regenerationtechniques is not critical for this invention.

In alternative embodiments, the invention provides for thetransformation of monocotyledonous plants using the nucleic acids of theinvention, including important cereals, see Hiei (1997) Plant Mol. Biol.35:205-218. See also, e.g., Horsch, Science (1984) 233:496; Fraley(1983) Proc. Natl. Acad. Sci. USA 80:4803; Thykjaer (1997) supra; Park(1996) Plant Mol. Biol. 32:1135-1148, discussing T-DNA integration intogenomic DNA. See also D'Halluin, U.S. Pat. No. 5,712,135, describing aprocess for the stable integration of a DNA comprising a gene that isfunctional in a cell of a cereal, or other monocotyledonous plant.

In alternative embodiments, the invention provides for regeneration andselection of whole plants capable of transmitting the incorporatedtarget gene to the next generation. Such regeneration techniques rely onmanipulation of certain phytohormones in a tissue culture growth medium,typically relying on a biocide and/or herbicide marker that has beenintroduced together with the desired nucleotide sequences. Plantregeneration from cultured protoplasts is described in Evans et al.,Protoplasts Isolation and Culture, Handbook of Plant Cell Culture, pp.124-176, MacMillilan Publishing Company, New York, 1983; and Binding,Regeneration of Plants, Plant Protoplasts, pp. 21-73, CRC Press, BocaRaton, 1985. Regeneration can also be obtained from plant callus,explants, organs, or parts thereof. Such regeneration techniques aredescribed generally in Klee (1987) Ann. Rev. of Plant Phys. 38:467-486.To obtain whole plants from transgenic tissues such as immature embryos,they can be grown under controlled environmental conditions in a seriesof media containing nutrients and hormones, a process known as tissueculture. Once whole plants are generated and produce seed, evaluation ofthe progeny begins.

In alternative embodiments, nucleic acids of the invention are definedand identified by nucleic acid hybridization reactions, the conditionsused to achieve a particular level of stringency will vary, depending onthe nature of the nucleic acids being hybridized. For example, thelength, degree of complementarity, nucleotide sequence composition(e.g., GC v. AT content), and nucleic acid type (e.g., RNA v. DNA) ofthe hybridizing regions of the nucleic acids can be considered inselecting hybridization conditions. An additional consideration iswhether one of the nucleic acids is immobilized, for example, on afilter.

In alternative embodiments, hybridizations are carried out underconditions of low stringency, moderate stringency or high stringency. Asan example of nucleic acid hybridization, a polymer membrane containingimmobilized denatured nucleic acids is first prehybridized for 30minutes at 45° C. in a solution consisting of 0.9 M NaCl, 50 mM NaH₂PO₄,pH 7.0, 5.0 mM Na₂EDTA, 0.5% SDS, 10×Denhardt's, and 0.5 mg/mlpolyriboadenylic acid. Approximately 2×107 cpm (specific activity4−9×108 cpm/ug) of 32P end-labeled oligonucleotide probe are then addedto the solution. After 12-16 hours of incubation, the membrane is washedfor 30 minutes at room temperature in 1×SET (150 mM NaCl, 20 mM Trishydrochloride, pH 7.8, 1 mM Na2EDTA) containing 0.5% SDS, followed by a30 minute wash in fresh 1×SET at Tm-10° C. for the oligonucleotideprobe. The membrane is then exposed to auto-radiographic film fordetection of hybridization signals.

In alternative embodiments, following hybridization, the filter iswashed to remove any non-specifically bound detectable probe. Thestringency used to wash the filters can also be varied depending on thenature of the nucleic acids being hybridized, the length of the nucleicacids being hybridized, the degree of complementarity, the nucleotidesequence composition (e.g., GC v. AT content), and the nucleic acid type(e.g., RNA v. DNA). Examples of progressively higher stringencycondition washes are as follows: 2×SSC, 0.1% SDS at room temperature for15 minutes (low stringency); 0.1×SSC, 0.5% SDS at room temperature for30 minutes to 1 hour (moderate stringency); 0.1×SSC, 0.5% SDS for 15 to30 minutes at between the hybridization temperature and 68° C. (highstringency); and 0.15M NaCl for 15 minutes at 72° C. (very highstringency). A final low stringency wash can be conducted in 0.1×SSC atroom temperature. The examples above are merely illustrative of one setof conditions that can be used to wash filters. One of skill in the artwould know that there are numerous recipes for different stringencywashes. Some other examples are given below.

6.19. Transgenic Non-Human Animals

In alternative embodiments, the invention provides transgenic non-humananimals comprising a nucleic acid, a polypeptide, an expression cassetteor vector or a transfected or transformed cell of the invention. Thetransgenic non-human animals can be, e.g., goats, rabbits, sheep, pigs,cows, rats and mice, comprising the nucleic acids of the invention.These animals can be used, e.g., as in vivo models to study ENZYMEactivity, or, as models to screen for modulators of ENZYME activity invivo. The coding sequences for the polypeptides to be expressed in thetransgenic non-human animals can be designed to be constitutive, or,under the control of tissue-specific, developmental-specific orinducible transcriptional regulatory factors. Transgenic non-humananimals can be designed and generated using any method known in the art.“Knockout animals” can also be used to practice the methods of theinvention. For example, in one aspect, the transgenic or modifiedanimals of the invention comprise a “knockout animal,” e.g., a “knockoutmouse,” engineered not to express or to be unable to express a nucleicacid or polypeptide.

Screening Methodologies and “On-line” Monitoring Devices

In practicing the methods of the invention, a variety of apparatus andmethodologies can be used to in conjunction with the polypeptides andnucleic acids of the invention, e.g., to screen polypeptides foractivity, to screen compounds as potential modulators of activity (e.g.,potentiation or inhibition of enzyme activity), for antibodies that bindto a polypeptide of the invention, for nucleic acids that hybridize to anucleic acid of the invention, and the like.

6.20. Immobilized Enzyme Solid Supports

In alternative embodiments, polypeptides of the invention, fragmentsthereof and nucleic acids that encode the enzymes and fragments can beaffixed to a solid support. This is often economical and efficient intheir use in industrial processes. For example, a consortium or cocktailof enzymes (or active fragments thereof), which are used in a specificchemical reaction, can be attached to a solid support and dunked into aprocess vat. The enzymatic reaction can occur. Then, the solid supportcan be taken out of the vat, along with the enzymes affixed thereto, forrepeated use. In one embodiment of the invention, an isolated nucleicacid of the invention is affixed to a solid support. In anotherembodiment of the invention, the solid support is selected from thegroup of a gel, a resin, a polymer, a ceramic, a glass, a microelectrodeand any combination thereof.

6.21. Methods of Immobilization

In alternative embodiments, any method known to one of skill in the artfor immobilizing enzymes or fragments thereof, or nucleic acids, onto asolid support is used to practice the invention. Some examples of suchmethods include, e.g., electrostatic droplet generation, electrochemicalmeans, via adsorption, via covalent binding, via cross-linking, via achemical reaction or process, via encapsulation, via entrapment, viacalcium alginate, or via poly (2-hydroxyethyl methacrylate). Likemethods are described in Methods in Enzymology, Immobilized Enzymes andCells, Part C. 1987. Academic Press. Edited by S. P. Colowick and N. O.Kaplan. Volume 136; and Immobilization of Enzymes and Cells. 1997.Humana Press. Edited by G. F. Bickerstaff. Series: Methods inBiotechnology, Edited by J. M. Walker.

6.22. Arrays, or “BioChips”

In alternative embodiments, nucleic acids or polypeptides of theinvention can be immobilized to or applied to an array. Arrays can beused to screen for or monitor libraries of compositions (e.g., smallmolecules, antibodies, nucleic acids, etc.) for their ability to bind toor modulate the activity of a nucleic acid or a polypeptide of theinvention. For example, in one aspect of the invention, a monitoredparameter is transcript expression of a gene. One or more, or, all thetranscripts of a cell can be measured by hybridization of a samplecomprising transcripts of the cell, or, nucleic acids representative ofor complementary to transcripts of a cell, by hybridization toimmobilized nucleic acids on an array, or “biochip.” By using an “array”of nucleic acids on a microchip, some or all of the transcripts of acell can be simultaneously quantified. Alternatively, arrays comprisinggenomic nucleic acid can also be used to determine the genotype of anewly engineered strain made by the methods of the invention.“Polypeptide arrays” can also be used to simultaneously quantify aplurality of proteins.

In practicing the methods of the invention, any known array and/ormethod of making and using arrays can be incorporated in whole or inpart, or variations thereof, as described, for example, in U.S. Pat.Nos. 6,277,628; 6,277,489; 6,261,776; 6,258,606; 6,054,270; 6,048,695;6,045,996; 6,022,963; 6,013,440; 5,965,452; 5,959,098; 5,856,174;5,830,645; 5,770,456; 5,632,957; 5,556,752; 5,143,854; 5,807,522;5,800,992; 5,744,305; 5,700,637; 5,556,752; 5,434,049; see also, e.g.,WO 99/51773; WO 99/09217; WO 97/46313; WO 96/17958; see also, e.g.,Johnston (1998) Curr. Biol. 8:R171-R174; Schummer (1997) Biotechniques23:1087-1092; Kern (1997) Biotechniques 23:120-124; Solinas-Toldo (1997)Genes, Chromosomes & Cancer 20:399-407; Bowtell (1999) Nature GeneticsSupp. 21:25-32. See also published U.S. patent applications Nos.20010018642; 20010019827; 20010016322; 20010014449; 20010014448;20010012537; 20010008765.

Polypeptides and Peptides

The invention provides isolated, synthetic or recombinant polypeptideshaving an amino acid sequence at least about 50%, 51%, 52%, 53%, 54%,55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%,69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%,83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%,97%, 98%, 99%, or more, or complete (100%) sequence identity to anexemplary polypeptides (e.g., enzymes) of the invention (or thesubsequences of, or enzymatically active fragments thereof), whichinclude SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ IDNO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ IDNO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ IDNO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ IDNO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ IDNO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58; SEQ IDNO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ IDNO:70, SEQ ID NO:72, SEQ ID NO:74, SEQ ID NO:76, SEQ ID NO:78, SEQ IDNO:80, SEQ ID NO:82, SEQ ID NO:84, SEQ ID NO:86, SEQ ID NO:88, SEQ IDNO:90, SEQ ID NO:92 and SEQ ID NO:94 and enzymatically active fragmentsthereof.

The invention further provides isolated, synthetic or recombinantnucleic acids encoding polypeptides of the invention.

In alternative invention, polypeptides and peptides of the invention aresynthetic or are recombinantly generated polypeptides. Peptides andproteins can be recombinantly expressed in vitro or in vivo. Thepeptides and polypeptides of the invention can be made and isolatedusing any method known in the art. Polypeptide and peptides of theinvention can also be synthesized, whole or in part, using chemicalmethods well known in the art. See e.g., Caruthers (1980) Nucleic AcidsRes. Symp. Ser. 215-223; Horn (1980) Nucleic Acids Res. Symp. Ser.225-232; Banga, A. K., Therapeutic Peptides and Proteins, Formulation,Processing and Delivery Systems (1995) Technomic Publishing Co.,Lancaster, Pa. For example, peptide synthesis can be performed usingvarious solid-phase techniques (see e.g., Roberge (1995) Science269:202; Merrifield (1997) Methods Enzymol. 289:3 13) and automatedsynthesis may be achieved, e.g., using the ABI 431A Peptide Synthesizer(Perkin Elmer) in accordance with the instructions provided by themanufacturer.

In alternative embodiments, “recombinant” polypeptides or proteins ofthe invention include (refer to) polypeptides or proteins produced byrecombinant DNA techniques; e.g., produced from cells transformed by anexogenous DNA construct encoding the desired polypeptide or protein. Inalternative embodiments, “Synthetic” nucleic acids (includingoligonucleotides), polypeptides or proteins of the invention includethose prepared by chemical synthesis, as described in detail herein. Inalternative embodiments, polypeptides or proteins of the inventioncomprise amino acids joined to each other by peptide bonds or modifiedpeptide bonds, i.e., peptide isosteres, and may contain modified aminoacids other than the 20 gene-encoded amino acids. The polypeptides maybe modified by either natural processes, such as post-translationalprocessing, or by chemical modification techniques that are well knownin the art. Modifications can occur anywhere in the polypeptide,including the peptide backbone, the amino acid side-chains and the aminoor carboxyl termini. It will be appreciated that the same type ofmodification may be present in the same or varying degrees at severalsites in a given polypeptide. Also a given polypeptide may have manytypes of modifications, for example, acetylation, acylation,ADP-ribosylation, amidation, covalent attachment of flavin, covalentattachment of a heme moiety, covalent attachment of a nucleotide ornucleotide derivative, covalent attachment of a lipid or lipidderivative, covalent attachment of a phosphatidylinositol, cross-linkingcyclization, disulfide bond formation, demethylation, formation ofcovalent cross-links, formation of cysteine, formation of pyroglutamate,formylation, gamma-carboxylation, glycosylation, GPI anchor formation,hydroxylation, iodination, methylation, myristolyation, oxidation,pegylation, proteolytic processing, phosphorylation, prenylation,racemization, selenoylation, sulfation, and transfer-RNA mediatedaddition of amino acids to protein such as arginylation.

In alternative embodiments, “synthetic” polypeptides or protein arethose prepared by chemical synthesis. Solid-phase chemical peptidesynthesis methods can also be used to synthesize the polypeptide orfragments of the invention. Such method have been known in the art sincethe early 1960's (Merrifield, R. B., J. Am. Chem. Soc., 85:2149-2154,1963) (See also Stewart, J. M. and Young, J. D., Solid Phase PeptideSynthesis, 2 ed., Pierce Chemical Co., Rockford, Ill., pp. 11-12)) andhave recently been employed in commercially available laboratory peptidedesign and synthesis kits (Cambridge Research Biochemicals).

In alternative aspects, peptides and polypeptides of the invention areglycosylated. The glycosylation can be added post-translationally eitherchemically or by cellular biosynthetic mechanisms, wherein the laterincorporates the use of known glycosylation motifs, which can be nativeto the sequence or can be added as a peptide or added in the nucleicacid coding sequence. The glycosylation can be O-linked or N-linked, or,a combination thereof.

In alternative aspects, peptides and polypeptides of the invention, asdefined above, comprise “mimetic” and “peptidomimetic” forms, either inpart or completely. In one aspect, the terms “mimetic” and“peptidomimetic” refer to a synthetic chemical compound which hassubstantially the same structural and/or functional characteristics ofthe polypeptides of the invention. The mimetic can be either entirelycomposed of synthetic, non-natural analogues of amino acids, or, is achimeric molecule of partly natural peptide amino acids and partlynon-natural analogs of amino acids. The mimetic can also incorporate anyamount of natural amino acid conservative substitutions as long as suchsubstitutions also do not substantially alter the mimetic's structureand/or activity. As with polypeptides of the invention which areconservative variants, routine experimentation will determine whether amimetic is within the scope of the invention, i.e., that its structureand/or function is not substantially altered. Thus, in one aspect, amimetic composition is within the scope of the invention if it has aENZYME activity.

Polypeptide mimetic compositions of the invention can contain anycombination of non-natural structural components. In alternative aspect,mimetic compositions of the invention include one or all of thefollowing three structural groups: a) residue linkage groups other thanthe natural amide bond (“peptide bond”) linkages; b) non-naturalresidues in place of naturally occurring amino acid residues; or c)residues which induce secondary structural mimicry, i.e., to induce orstabilize a secondary structure, e.g., a beta turn, gamma turn, betasheet, alpha helix conformation, and the like. For example, apolypeptide of the invention can be characterized as a mimetic when allor some of its residues are joined by chemical means other than naturalpeptide bonds. Individual peptidomimetic residues can be joined bypeptide bonds, other chemical bonds or coupling means, such as, e.g.,glutaraldehyde, N-hydroxysuccinimide esters, bifunctional maleimides,N,N′-dicyclohexylcarbodiimide (DCC) or N,N′-diisopropyl-carbodiimide(DIC) Linking groups that can be an alternative to the traditional amidebond (“peptide bond”) linkages include, e.g., ketomethylene (e.g.,—C(═O)—CH2- for —C(═O)—NH—), aminomethylene (CH2-NH), ethylene, olefin(CH═CH), ether (CH2-O), thioether (CH2-S), tetrazole (CN4-), thiazole,retroamide, thioamide, or ester (see, e.g., Spatola (1983) in Chemistryand Biochemistry of Amino Acids, Peptides and Proteins, Vol. 7, pp267-357, “Peptide Backbone Modifications,” Marcell Dekker, NY).

In alternative embodiments, a polypeptide of the invention can also becharacterized as a mimetic by containing all or some non-naturalresidues in place of naturally occurring amino acid residues.Non-natural residues are well described in the scientific and patentliterature; a few exemplary non-natural compositions useful as mimeticsof natural amino acid residues and guidelines are described below.Mimetics of aromatic amino acids can be generated by replacing by, e.g.,D- or L-naphylalanine; D- or L-phenylglycine; D- or L-2 thieneylalanine;D- or L-1, -2,3-, or 4-pyreneylalanine; D- or L-3 thieneylalanine; D- orL-(2-pyridinyl)-alanine; D- or L-(3-pyridinyl)-alanine; D- orL-(2-pyrazinyl)-alanine; D- or L-(4-isopropyl)-phenylglycine;D-(trifluoromethyl)-phenylglycine; D-(trifluoromethyl)-phenylalanine;D-p-fluoro-phenylalanine; D- or L-p-biphenylphenylalanine; K- orL-p-methoxy-biphenylphenylalanine; D- or L-2-indole(alkyl)alanines; and,D- or L-alkylainines, where alkyl can be substituted or unsubstitutedmethyl, ethyl, propyl, hexyl, butyl, pentyl, isopropyl, iso-butyl,sec-isotyl, iso-pentyl, or a non-acidic amino acids. Aromatic rings of anon-natural amino acid include, e.g., thiazolyl, thiophenyl, pyrazolyl,benzimidazolyl, naphthyl, furanyl, pyrrolyl, and pyridyl aromatic rings.

In alternative embodiments, mimetics of acidic amino acids can begenerated by substitution by, e.g., non-carboxylate amino acids whilemaintaining a negative charge; (phosphono)alanine; sulfated threonine.Carboxyl side groups (e.g., aspartyl or glutamyl) can also beselectively modified by reaction with carbodiimides (R′—N—C—N—R′) suchas, e.g., 1-cyclohexyl-3(2-morpholinyl-(4-ethyl) carbodiimide or1-ethyl-3(4-azonia-4,4-dimetholpentyl) carbodiimide. Aspartyl orglutamyl can also be converted to asparaginyl and glutaminyl residues byreaction with ammonium ions. Mimetics of basic amino acids can begenerated by substitution with, e.g., (in addition to lysine andarginine) the amino acids ornithine, citrulline, or (guanidino)-aceticacid, or (guanidino)alkyl-acetic acid, where alkyl is defined above.Nitrile derivative (e.g., containing the CN-moiety in place of COOH) canbe substituted for asparagine or glutamine Asparaginyl and glutaminylresidues can be deaminated to the corresponding aspartyl or glutamylresidues. Arginine residue mimetics can be generated by reacting arginylwith, e.g., one or more conventional reagents, including, e.g.,phenylglyoxal, 2,3-butanedione, 1,2-cyclo-hexanedione, or ninhydrin,which for these reagents it may be preferable to use alkalineconditions. Tyrosine residue mimetics can be generated by reactingtyrosyl with, e.g., aromatic diazonium compounds or tetranitromethane.N-acetylimidizol and tetranitromethane can be used to form O-acetyltyrosyl species and 3-nitro derivatives, respectively. Cysteine residuemimetics can be generated by reacting cysteinyl residues with, e.g.,alpha-haloacetates such as 2-chloroacetic acid or chloroacetamide andcorresponding amines; to give carboxymethyl or carboxyamidomethylderivatives. Cysteine residue mimetics can also be generated by reactingcysteinyl residues with, e.g., bromo-trifluoroacetone,alpha-bromo-beta-(5-imidozoyl) propionic acid; chloroacetyl phosphate,N-alkylmaleimides, 3-nitro-2-pyridyl disulfide; methyl 2-pyridyldisulfide; p-chloromercuribenzoate; 2-chloromercuri-4 nitrophenol; or,chloro-7-nitrobenzo-oxa-1,3-diazole. Lysine mimetics can be generated(and amino terminal residues can be altered) by reacting lysinyl with,e.g., succinic or other carboxylic acid anhydrides. Lysine and otheralpha-amino-containing residue mimetics can also be generated byreaction with imidoesters, such as methyl picolinimidate, pyridoxalphosphate, pyridoxal, chloroborohydride, trinitro-benzenesulfonic acid,O-methylisourea, 2,4, pentanedione, and transamidase-catalyzed reactionswith glyoxylate. Mimetics of methionine can be generated by reactionwith, e.g., methionine sulfoxide. Mimetics of proline include, e.g.,pipecolic acid, thiazolidine carboxylic acid, 3- or 4-hydroxy proline,dehydroproline, 3- or 4-methylproline, or 3,3,-dimethylproline.Histidine residue mimetics can be generated by reacting histidyl with,e.g., diethylprocarbonate or para-bromophenacyl bromide. Other mimeticsinclude, e.g., those generated by hydroxylation of proline and lysine;phosphorylation of the hydroxyl groups of seryl or threonyl residues;methylation of the alpha-amino groups of lysine, arginine and histidine;acetylation of the N-terminal amine; methylation of main chain amideresidues or substitution with N-methyl amino acids; or amidation ofC-terminal carboxyl groups.

In alternative embodiments, a residue, e.g., an amino acid, of apolypeptide of the invention can also be replaced by an amino acid (orpeptidomimetic residue) of the opposite chirality. Thus, any amino acidnaturally occurring in the L-configuration (which can also be referredto as the R or S, depending upon the structure of the chemical entity)can be replaced with the amino acid of the same chemical structural typeor a peptidomimetic, but of the opposite chirality, referred to as theD-amino acid, but also can be referred to as the R- or S-form.

In alternative embodiments, the invention provides methods for modifyingthe polypeptides of the invention by either natural processes, such aspost-translational processing (e.g., phosphorylation, acylation, etc),or by chemical modification techniques, and the resulting modifiedpolypeptides. Modifications can occur anywhere in the polypeptide,including the peptide backbone, the amino acid side-chains and the aminoor carboxyl termini. It will be appreciated that the same type ofmodification may be present in the same or varying degrees at severalsites in a given polypeptide. Also a given polypeptide may have manytypes of modifications. Modifications include acetylation, acylation,ADP-ribosylation, amidation, covalent attachment of flavin, covalentattachment of a heme moiety, covalent attachment of a nucleotide ornucleotide derivative, covalent attachment of a lipid or lipidderivative, covalent attachment of a phosphatidylinositol, cross-linkingcyclization, disulfide bond formation, demethylation, formation ofcovalent cross-links, formation of cysteine, formation of pyroglutamate,formylation, gamma-carboxylation, glycosylation, GPI anchor formation,hydroxylation, iodination, methylation, myristolyation, oxidation,pegylation, proteolytic processing, phosphorylation, prenylation,racemization, selenoylation, sulfation, and transfer-RNA mediatedaddition of amino acids to protein such as arginylation. See, e.g.,Creighton, T. E., Proteins—Structure and Molecular Properties 2nd Ed.,W.H. Freeman and Company, New York (1993); Posttranslational CovalentModification of Proteins, B. C. Johnson, Ed., Academic Press, New York,pp. 1-12 (1983).

In alternative embodiments, provides polypeptides having no or modifiedsignal sequences (also called signal peptides (SPs), or leaderpeptides), or heterologous signal sequences. The polypeptides of theinvention also can have no or modified or heterologous prepro domainsand/or catalytic domains (CDs). The modified or heterologous SPs, preprodomains and/or CDs incorporated in a polypeptide the invention can bepart of a fusion protein, e.g., as a heterologous domain in a chimericprotein, or added by a chemical linking agent. For example, an enzyme ofthe invention can comprise a heterologous SP and/or prepro in a vector,e.g., a pPIC series vector (Invitrogen, Carlsbad, Calif.).

In alternative embodiments, polypeptides of the invention compriseepitopes or purification tags, signal sequences or other fusionsequences, etc. In one aspect, polypeptides of the invention can befused to a random peptide to form a fusion polypeptide. By “fused” or“operably linked” herein is meant that the random peptide and thepolypeptide are linked together, in such a manner as to minimize thedisruption to the stability of polypeptide activity. The fusionpolypeptide (or fusion polynucleotide encoding the fusion polypeptide)can comprise further components as well, including multiple peptides atmultiple loops.

In one aspect, polypeptides of the invention are chimeric polypeptides,e.g., comprising heterologous SPs, carbohydrate binding modules, enzymecatalytic domains, linkers and/or non-cellulase catalytic domains. Theinvention provides a means for generating chimeric polypeptides whichmay encode biologically active hybrid polypeptides (e.g.,hybridenzymes). In one aspect, the original polynucleotides encodebiologically active polypeptides.

In one aspect, the instant invention provides a method (and productsthereof) of producing stabilized aqueous liquid formulations havingpolypeptide activity that exhibit increased resistance to heatinactivation of the enzyme activity and which retain their activityduring prolonged periods of storage. The liquid formulations arestabilized by means of the addition of urea and/or a polyol such assorbitol and glycerol as stabilizing agent. Also provided are feedpreparations for monogastric animals and methods for the productionthereof that result from the use of such stabilized aqueous liquidformulations. Additional details regarding this approach are in thepublic literature and/or are known to the skilled artisan. In aparticular non-limiting exemplification, such publicly availableliterature includes EP 0626010 (WO 9316175 A1) (Barendse et al.),although references in the publicly available literature do not teachthe inventive molecules of the instant application.

6.23. Antibodies and Antibody-Based Screening Methods

The invention provides isolated, synthetic or recombinant antibodiesthat specifically bind to a polypeptide of the invention. Theseantibodies can be used to isolate, identify or quantify polypeptides ofthe invention or related polypeptides. These antibodies can be used toinhibit the activity of an enzyme of the invention. These antibodies canbe used to isolated polypeptides related to those of the invention,e.g., related enzymes.

Antibodies of the invention can comprise a peptide or polypeptidederived from, modeled after or substantially encoded by animmunoglobulin gene or immunoglobulin genes, or fragments thereof,capable of specifically binding an antigen or epitope, see, e.g.Fundamental Immunology, Third Edition, W. E. Paul, ed., Raven Press,N.Y. (1993); Wilson (1994) J. Immunol. Methods 175:267-273; Yarmush(1992) J. Biochem. Biophys. Methods 25:85-97. The term antibody includesantigen-binding portions, i.e., “antigen binding sites,” (e.g.,fragments, subsequences, complementarity determining regions (CDRs))that retain capacity to bind antigen, including (i) a Fab fragment, amonovalent fragment consisting of the VL, VH, CL and CH1 domains; (ii) aF(ab′)2 fragment, a bivalent fragment comprising two Fab fragmentslinked by a disulfide bridge at the hinge region; (iii) a Fd fragmentconsisting of the VH and CH1 domains; (iv) a Fv fragment consisting ofthe VL and VH domains of a single arm of an antibody, (v) a dAb fragment(Ward et al., (1989) Nature 341:544-546), which consists of a VH domain;and (vi) an isolated complementarity determining region (CDR). Singlechain antibodies are also included by reference in the term “antibody.”

The antibodies can be used in immunoprecipitation, staining (e.g.,FACS), immunoaffinity columns, and the like. If desired, nucleic acidsequences encoding for specific antigens can be generated byimmunization followed by isolation of polypeptide or nucleic acid,amplification or cloning and immobilization of polypeptide onto an arrayof the invention. Alternatively, the methods of the invention can beused to modify the structure of an antibody produced by a cell to bemodified, e.g., an antibody's affinity can be increased or decreased.Furthermore, the ability to make or modify antibodies can be a phenotypeengineered into a cell by the methods of the invention.

Methods of immunization, producing and isolating antibodies (polyclonaland monoclonal) are known to those of skill in the art and described inthe scientific and patent literature, see, e.g., Coligan, CURRENTPROTOCOLS IN IMMUNOLOGY, Wiley/Greene, NY (1991); Stites (eds.) BASICAND CLINICAL IMMUNOLOGY (7th ed.) Lange Medical Publications, Los Altos,Calif. (“Stites”); Goding, MONOCLONAL ANTIBODIES: PRINCIPLES ANDPRACTICE (2d ed.) Academic Press, New York, N.Y. (1986); Kohler (1975)Nature 256:495; Harlow (1988) ANTIBODIES, A LABORATORY MANUAL, ColdSpring Harbor Publications, New York. Antibodies also can be generatedin vitro, e.g., using recombinant antibody binding site expressing phagedisplay libraries, in addition to the traditional in vivo methods usinganimals. See, e.g., Hoogenboom (1997) Trends Biotechnol. 15:62-70; Katz(1997) Annu. Rev. Biophys. Biomol. Struct. 26:27-45.

The polypeptides can be used to generate antibodies which bindspecifically to the polypeptides of the invention. The resultingantibodies may be used in immunoaffinity chromatography procedures toisolate or purify the polypeptide or to determine whether thepolypeptide is present in a biological sample. In such procedures, aprotein preparation, such as an extract, or a biological sample iscontacted with an antibody capable of specifically binding to one of thepolypeptides of the invention.

6.24. Kits

The invention provides kits comprising the compositions, e.g., nucleicacids, expression cassettes, vectors, cells, polypeptides (e.g.,celluloses or a cellobiohydrolases) and/or antibodies of the invention.The kits also can contain instructional material teaching themethodologies and industrial uses of the invention, as described herein.

The polypeptides of the invention may also be used to generateantibodies which bind specifically to the enzyme polypeptides orfragments. The resulting antibodies may be used in immunoaffinitychromatography procedures to isolate or purify the polypeptide or todetermine whether the polypeptide is present in a biological sample. Insuch procedures, a protein preparation, such as an extract, or abiological sample is contacted with an antibody capable of specificallybinding to one of a polypeptide of the invention, sequencessubstantially identical thereto, or fragments of the foregoingsequences.

6.25. Enzyme Delivery Matrices

In alternative embodiments, the invention provides an edible pelletizedenzyme delivery matrix and method of use for delivery of a polypeptideof the invention to an animal, for example as a nutritional supplement.The enzyme delivery matrix readily releases a polypeptide of theinvention, such as an enzyme of the invention, in aqueous media, suchas, for example, the digestive fluid of an animal. The invention enzymedelivery matrix is prepared from a granulate edible carrier selectedfrom such components as grain germ that is spent of oil, hay, alfalfa,timothy, soy hull, sunflower seed meal, wheat meal, and the like, thatreadily disperse the recombinant enzyme contained therein into aqueousmedia. In use, the edible pelletized enzyme delivery matrix isadministered to an animal to delivery of polypeptide of the invention tothe animal. Suitable grain-based substrates may comprise or be derivedfrom any suitable edible grain, such as wheat, corn, soy, sorghum,alfalfa, barley, and the like. An exemplary grain-based substrate is acorn-based substrate. The substrate may be derived from any suitablepart of the grain, e.g., a grain germ, approved for animal feed use,such as corn germ that is obtained in a wet or dry milling process. Thegrain germ can comprise spent germ, which is grain germ from which oilhas been expelled, such as by pressing or hexane or other solventextraction. Alternatively, the grain germ is expeller extracted, thatis, the oil has been removed by pressing.

6.26. Industrial/Upscale Expression of Enzymes of the Invention

In alternative embodiments, the invention provides for upscaleproduction of polypeptides of the invention. Any known industrialprocess, bioreactor and/or cell-based expression system can be used topractice the invention. In one aspect, commercial (e.g., “upscaled”)enzyme production systems are used, and this invention can use anypolypeptide production system known the art, including any cell-basedexpression system, which include numerous strains, including anyeukaryotic or prokaryotic system, including any insect, microbial,yeast, bacterial and/or fungal expression system; these alternativeexpression systems are well known and discussed in the literature andall are contemplated for commercial use for producing and using theenzymes of the invention. In alternative embodiments, nucleic acids ofthe invention are expressed in an Aspergillus, e.g., an Aspergillusniger, a Pichia, e.g., a Pichia pastoris, a Schizosaccharomyces, e.g., aSchizosaccharomyces pombe, and/or a Pseudomonas, e.g., a Pseudomonasfluorescens; e.g., to express polypeptides of the invention in anindustrial, or upscale, production system. For example, Bacillus speciescan be used for industrial production (see, e.g., Canadian Journal ofMicrobiology, 2004 January, 50(1):1-17). Alternatively, Streptomycesspecies, such as S. lividans, S. coelicolor, S. limosus, S. rimosus, S.roseosporus, and S. lividans can be used for industrial and sustainableproduction hosts (see, e.g., Appl Environ Microbiol. 2006 August; 72(8):5283-5288). Aspergillus strains such as Aspergillus phoenicis, A. nigerand A. carbonarius can be used to practice this invention, e.g., toproduce an enzyme, such as a beta-glucosidase, of this invention (see,e.g., World Journal of Microbiology and Biotechnology, 2001,17(5):455-461). Any Fusarium sp. can be used in an expression system topractice this invention, including e.g., Fusarium graminearum; see e.g.,Royer et al. Bio/Technology 13:1479-1483 (1995). Any Aspergillus sp. canbe used in an expression system to practice this invention, includinge.g., A. nidulans; A. fumigatus; A. niger or A. oryzae. For example, thegenome for A. niger CBS513.88, a parent of commercially used enzymeproduction strains, was recently sequenced (see, e.g., Nat. Biotechnol.2007 February, 25(2):221-31) and can be used as an expression system topractice the invention. Similarly, the genomic sequencing of Aspergillusoryzae was recently completed (Nature. 2005 Dec. 22, 438(7071):1157-61).For alternative fungal expression systems that can be used to practicethis invention, e.g., to express enzymes for use in industrialapplications, such as biofuel production, see e.g., Advances in FungalBiotechnology for Industry, Agriculture, and Medicine. Edited by Jan S.Tkacz & Lene Lange. 2004. Kluwer Academic & Plenum Publishers, New York;and e.g., Handbook of Industrial Mycology. Edited by Zhiqiang An. 24Sep. 2004. Mycology Series No. 22. Marcel Dekker, New York; and e.g.,Talbot (2007) “Fungal genomics goes industrial”, Nature Biotechnology25(5):542; and in USPNs 4,885,249; 5,866,406; and international patentpublication WO/2003/012071.

Cells for expressing enzymes of this invention can be manipulated e.g.,to increase efficiencies and/or yields, etc., as described e.g., in U.S.Pat. No. 7,517,668; U.S. Pat. App. Pub. Nos. 20030119013; 20100120029;20060235200. Specific expression vehicles and/or transcriptionalregulatory or other motifs (e.g., to facilitate secretion) can be usedto e.g., maximize efficiencies and/or yields, etc., as described e.g.,in U.S. Pat. Nos. 5,198,345; 5,364,770; 5,578,463; 5,536,661; 6,255,115;6,080,564, describing a method for inactivating undesired acid labileproteases which are expressed into culture medium simultaneously withdesired enzymes by Aspergillus; U.S. Pat. No. 5,324,660, describingstrains of Pichia which are deficient in proteolytic activity; U.S. Pat.App. Pub. Nos. 20060105425; 20080227148; 20030013154, 7,741,075 and7,271,255, describing Pichia secretory leaders for protein expression.See also e.g., U.S. Pat. App. Pub. No. 20080044858 describing methods ofproducing a biological substances in Aspergillus; 6,316,245, describinga fermentation process to have a high productivity with a novel mutantof Pichia sp.; 20100175147, describing a Pichia expression system; U.S.Pat. No. 6,451,063, describing production of cellulases for industrialuses.

For example, in one embodiment, enzymes are produced as described inU.S. Pat. No. 7,695,949, which describes a process that uses afermentation medium containing a recombinantly-produced microorganismthat over-produces a fermentation product and contains a mutation whichcauses auxotrophic growth of the microorganism, and the auxotrophywithin the microorganism does not compromise the ability of themicroorganism to produce the fermentation product. The medium is thensupplied in excess with all substrates required for production of thefermentation product and in growth limiting amounts with a substratecomplementing the auxotrophy. In one embodiment, enzymes are produced asdescribed in U.S. Pat. App. Pub. No. 20090280212, describing a method ofadjusting productivity of enzymes in a filamentous fungus cultureproduct; or U.S. Pat. No. 6,893,849 describing a Pichia expressionsystem. Any culture medium known in the art can be used, e.g., asdescribed in U.S. Pat. App. Pub. No. 20100062513.

In one embodiment, any bioreactor, culture vessel or cell growth productof manufacture can be used to practice the invention, e.g., as describedin U.S. Pat. Nos. 6,001,643; 6,642,019; 7,112,441; 7,163,821; 7,604,987,which describes e.g. a chamber for containing cells or tissue cultureswithin a culture medium; 7,749,750; and U.S. Pat. App. Pub. Nos.20040152186; 20030040104, describing an automated cell management systemwhich can be programmed to perform and control various operations of theessential phases of cell culturing, of cell culture manipulation, and ofcell culture evaluation; 20100062483; 20090068739; 20080233631.

6.27. Enzymatic Processes for Sugarcane Bagasse

In alternative embodiments, polypeptides of the invention are used toenzymatically process (hydrolyze) sugarcane (Saccharum), sugarcane parts(e.g., cane tops) and/or sugarcane bagasse, i.e., for sugarcanedegradation, or for biomass processing, and polynucleotides encodingthese enzymes, and making and using these polynucleotides andpolypeptides. The invention provides polypeptides and methods forprocessing lignocellulosic residues, including sugarcane bagasse, or anywaste product of the sugar milling or related industries, into alignocellulosic hydrolysis product, which itself can be a biofuel orwhich can be further processed to become a biofuel, including liquid orgas fuels. Because the invention provides enzymes and methods for sugarcane processing, it also provides methods for making (methods for theproduction of) edible sugar, garapa, rapadura (papelón), falernum,molasses, rum, cachaça, in addition to alcohols (for any purpose) and/orbiofuels, e.g., bioethanol. Thus, the invention also provides ediblesugar, garapa, rapadura (papelón), falernum, molasses, rum, cachaça,alcohols, biofuels, e.g., bioethanol and the like, and theirintermediate, comprising a polypeptide of the invention.

In some aspects, are several advantages to using sugarcane, e.g.,bagasse, as a substrate for bioconversion:

-   1. It has high carbohydrate content (cellulose, 40-50%, and    hemicellulose, 20-30%);-   2. It is collected at the site of processing;-   3. It is a cheap substrate, and there is a constant, although    seasonal supply generated within the sugarcane industry.

The invention provides polypeptides and methods for hydrolyzingcellulose and hemicellulose polysaccharides in sugarcane, e.g., bagasse,which are associated with lignin, which can act as a barrier shieldingthe polysaccharides from attack by microorganisms and their associatedenzyme systems. Because of the structural characteristics oflignocellulose, such as its lignin barrier and cellulose crystallinity,in one aspect a pretreatment process is used to enhance the access ofenzyme(s) of this invention to the polysaccharide components in abiomass (a bagasse) to increase the conversion yields into the buildingblock monosaccharides, such as hexose and pentose sugars. In oneexemplary system of this invention using enzyme(s) of this invention,sugars produced are efficiently fermented to ethanol, and burningunhydrolyzed carbohydrate plus lignin provides enough steam to fuel thesugar mills.

In alternative aspects, the processes of the invention use variouspretreatments, which can be grouped into three categories: physical,chemical, and multiple (physical+chemical). Any chemicals can be used asa pretreatment agent, e.g., acids, alkalis, gases, cellulose solvents,alcohols, oxidizing agents and reducing agents. Among these chemicals,alkali is the most popular pretreatment agent because it is relativelyinexpensive and results in less cellulose degradation. The commonalkalis sodium hydroxide and lime also can be used as pretreatmentagents. Although sodium hydroxide increases biomass digestibilitysignificantly, it is difficult to recycle, is relatively expensive, andis dangerous to handle. In contrast, lime has many advantages: it issafe and very inexpensive, and can be recovered by carbonating washwater with carbon dioxide.

In one aspect, the invention provides a multi-enzyme system (includingat least one enzyme of this invention) that can hydrolyzepolysaccharides in a sugarcane, e.g., bagasse, component of sugarcaneprocessed in sugar mills. In one aspect, the sugarcane, e.g., bagasse,is processed by an enzyme of the invention made by an organism (e.g.,transgenic animal, plants, transformed microorganism) and/or byproduct(e.g., harvested plant, fruit, seed) expressing an enzyme of theinvention. In one aspect, the enzyme is a recombinant enzyme made by theplant or biomass which is to be processed to a fuel, e.g., the inventionprovides a transgenic sugarcane bagasse comprising an enzyme of theinvention. In one aspect, these compositions and products used inmethods of the invention comprising chemical cycles for natural biomassconversion, e.g., for the hydrolysis of a biomass to make a biofuel,e.g., bioethanol, biopropanol, bio-butanol, biomethanol, a syntheticfuel in the form of a liquid or a gas, such as a “syngas”.

In one aspect, the invention provides a biofuel, e.g., a biogas,produced by the process of anaerobic digestion of organic material byanaerobes, wherein the process comprises use of an enzyme of theinvention or a method of the invention. This biofuel, e.g., a biogas,can be produced either from biodegradable waste materials or by the useof energy crops fed into anaerobic digesters to supplement gas yields.The solid output, digestate, can also be used as a biofuel.

In one aspect, the invention provides a biofuel, e.g., a biogas,comprising a methane, wherein the process comprises use of an enzyme ofthe invention or a method of the invention. This biofuel, e.g., abiogas, can be recovered in industrial anaerobic digesters andmechanical biological treatment systems. Landfill gas can be furtherprocessed using an enzyme of this invention or a process of thisinvention; before processing landfill gas can be a less clean form ofbiogas produced in landfills through naturally occurring anaerobicdigestion. Paradoxically if landfill gas is allowed to escape into theatmosphere it is a potent greenhouse gas.

The invention provides methods for making biologically produced oils andgases from various wastes, wherein the process comprises use of anenzyme of the invention or a method of the invention. In one aspect,these methods comprise thermal depolymerization of waste to extractmethane and other oils similar to petroleum; or, e.g., a bioreactorsystem that utilizes nontoxic photosynthetic algae to take insmokestacks flue gases and produce biofuels such as biodiesel, biogasand a dry fuel comparable to coal, e.g., as designed by GreenFuelTechnologies Corporation, of Cambridge, Mass.

The invention provides methods for making biologically produced oils,including crude oils, and gases that can be used in diesel engines,wherein the process comprises use of an enzyme of the invention or amethod of the invention. In one aspect, these methods can refinepetroleum, e.g., crude oils, into kerosene, petroleum, diesel and otherfractions.

The invention provides methods (using an enzyme of the invention or amethod of the invention) for making biologically produced oils from:

-   -   Straight vegetable oil (SVO).    -   Waste vegetable oil (WVO)—waste cooking oils and greases        produced in quantity mostly by commercial kitchens.    -   Biodiesel obtained from transesterification of animal fats and        vegetable oil, directly usable in petroleum diesel engines.    -   Biologically derived crude oil, together with biogas and carbon        solids via the thermal depolymerization of complex organic        materials including non oil based materials; for example, waste        products such as old tires, offal, wood and plastic.    -   Pyrolysis oil; which may be produced out of biomass, wood waste        etc. using heat only in the flash pyrolysis process (the oil may        have to be treated before using in conventional fuel systems or        internal combustion engines).    -   Wood, charcoal, and dried dung.

6.28. Animal Feeds and Food or Feed Additives

In alternative embodiments, addition to providing dietary aids orsupplements, or food supplements and additives for human use, theinvention also provides compositions and methods for treating animalfeeds and foods and food or feed additives using a polypeptide of theinvention, e.g., a protein having a lignocellulosic activity, e.g., acellobiohydrolase enzyme of the invention, and/or the antibodies of theinvention. The invention provides animal feeds, foods, and additivescomprising the lignocellulosic enzymes of the invention and/orantibodies of the invention. The animal can be any farm animal or anyanimal.

In alternative embodiments, the animal feed additive of the inventionmay be a granulated enzyme product that may readily be mixed with feedcomponents. Alternatively, feed additives of the invention can form acomponent of a pre-mix. The granulated enzyme product of the inventionmay be coated or uncoated. The particle size of the enzyme granulatescan be compatible with that of feed and pre-mix components. Thisprovides a safe and convenient mean of incorporating enzymes into feeds.Alternatively, the animal feed additive of the invention may be astabilized liquid composition. This may be an aqueous or oil-basedslurry. See, e.g., U.S. Pat. No. 6,245,546.

In alternative embodiments, the lignocellulosic enzyme of the presentinvention, in the modification of animal feed or a food, can process thefood or feed either in vitro (by modifying components of the feed orfood) or in vivo. Polypeptides of the invention can be added to animalfeed or food compositions.

In alternative embodiments, an enzyme of the invention is added incombination with another enzyme, e.g., beta-galactosidases, catalases,laccases, other cellulases, endoglycosidases, endo-beta-1,4-laccases,amyloglucosidases, other glucosidases, glucose isomerases,glycosyltransferases, lipases, phospholipases, lipooxygenases,beta-laccases, endo-beta-1,3(4)-laccases, cutinases, peroxidases,amylases, glucoamylases, pectinases, reductases, oxidases,decarboxylases, phenoloxidases, ligninases, pullulanases, arabinanases,hemicellulases, mannanases, xylolaccases, xylanases, pectin acetylesterases, rhamnogalacturonan acetyl esterases, proteases, peptidases,proteinases, polygalacturonases, rhamnogalacturonases, galactanases,pectin lyases, transglutaminases, pectin methylesterases,cellobiohydrolases, and/or glucose oxidases. These enzyme digestionproducts are more digestible by the animal. Thus, the lignocellulosicenzyme, e.g., glycosyl hydrolase, cellulase, endoglucanase,cellobiohydrolase, beta-glucosidase, xylanase, mannanse, β-xylosidaseand/or arabinofuranosidase enzymes of the invention can contribute tothe available energy of the feed or food, or to the digestibility of thefood or feed by breaking down cellulose.

In alternative embodiments, a lignocellulosic enzyme, e.g., celluloseor, cellobiohydrolase, enzyme of the invention can be supplied byexpressing the enzymes directly in transgenic feed crops (as, e.g.,transgenic plants, seeds and the like), such as grains, cereals, corn,soy bean, rape seed, lupin and the like. As discussed above, theinvention provides transgenic plants, plant parts and plant cellscomprising a nucleic acid sequence encoding a polypeptide of theinvention. In one aspect, the nucleic acid is expressed such that thelignocellulosic enzyme of the invention is produced in recoverablequantities. The lignocellulosic enzyme can be recovered from any plantor plant part. Alternatively, the plant or plant part containing therecombinant polypeptide can be used as such for improving the quality ofa food or feed, e.g., improving nutritional value, palatability, etc.

In one aspect, the enzyme delivery matrix of the invention is in theform of discrete plural particles, pellets or granules. By “granules” ismeant particles that are compressed or compacted, such as by apelletizing, extrusion, or similar compacting to remove water from thematrix. Such compression or compacting of the particles also promotesintraparticle cohesion of the particles. For example, the granules canbe prepared by pelletizing the grain-based substrate in a pellet mill.The pellets prepared thereby are ground or crumbled to a granule sizesuitable for use as an adjuvant in animal feed. Since the matrix isitself approved for use in animal feed, it can be used as a diluent fordelivery of enzymes in animal feed.

In alternative embodiments, the lignocellulosic enzyme is contained inthe invention enzyme delivery matrix and methods is a thermostable thelignocellulosic enzyme, as described herein, so as to resistinactivation of the lignocellulosic enzyme during manufacture whereelevated temperatures and/or steam may be employed to prepare thepalletized enzyme delivery matrix. During digestion of feed containingthe invention enzyme delivery matrix, aqueous digestive fluids willcause release of the active enzyme. Other types of thermostable enzymesand nutritional supplements that are thermostable can also beincorporated in the delivery matrix for release under any type ofaqueous conditions.

In alternative embodiments, a coating is applied to the enzyme matrixparticles for many different purposes, such as to add a flavor ornutrition supplement to animal feed, to delay release of animal feedsupplements and enzymes in gastric conditions, and the like. In oneaspect, the coating is applied to achieve a functional goal, forexample, whenever it is desirable to slow release of the enzyme from thematrix particles or to control the conditions under which the enzymewill be released. The composition of the coating material can be suchthat it is selectively broken down by an agent to which it issusceptible (such as heat, acid or base, enzymes or other chemicals).Alternatively, two or more coatings susceptible to different suchbreakdown agents may be consecutively applied to the matrix particles.

In alternative embodiments, the invention provides processes forpreparing an enzyme-releasing matrix. In alternative embodiments, theprocess comprises providing discrete plural particles of a grain-basedsubstrate in a particle size suitable for use as an enzyme-releasingmatrix, wherein the particles comprise a lignocellulosic enzyme, e.g., aglycosyl hydrolase, cellulase, endoglucanase, cellobiohydrolase,beta-glucosidase, xylanase, mannanse, β-xylosidase and/orarabinofuranosidase enzyme encoded by an amino acid sequence of theinvention. In one aspect, the process includes compacting or compressingthe particles of enzyme-releasing matrix into granules, which most inone aspect is accomplished by pelletizing. The mold inhibitor andcohesiveness agent, when used, can be added at any suitable time, and inone aspect are mixed with the grain-based substrate in the desiredproportions prior to pelletizing of the grain-based substrate. Moisturecontent in the pellet mill feed in one aspect is in the ranges set forthabove with respect to the moisture content in the finished product, andin one aspect is about 14-15%. In one aspect, moisture is added to thefeedstock in the form of an aqueous preparation of the enzyme to bringthe feedstock to this moisture content. The temperature in the pelletmill in one aspect is brought to about 82° C. with steam. The pelletmill may be operated under any conditions that impart sufficient work tothe feedstock to provide pellets. The pelleting process itself is acost-effective process for removing water from the enzyme-containingcomposition.

In alternative embodiments, the compositions and methods of theinvention can be practiced in conjunction with administration ofprebiotics, which are high molecular weight sugars, e.g.,fructo-oligosaccharides (FOS); galacto-oligosaccharides (GOS), GRAS(Generally Recognized As Safe) material. These prebiotics can bemetabolized by some probiotic lactic acid bacteria (LAB). They arenon-digestible by the majority of intestinal microbes.

6.29. Treating Foods and Food Processing

In alternative embodiments, the invention provides foods and feedscomprising enzymes of the invention, and methods for using enzymes ofthe invention in processing foods and feeds. Cellulases, e.g.,cellobiohydrolase enzymes, of the invention have numerous applicationsin food processing industry. The invention provides methods forhydrolyzing cellulose-comprising compositions, including, e.g., a plantcell, a bacterial cell, a yeast cell, an insect cell, or an animal cell,or any plant or plant part, or any food or feed, a waste product and thelike.

For example, the invention provides feeds or foods comprising alignocellulosic enzyme of the invention, e.g., in a feed, a liquid,e.g., a beverage (such as a fruit juice or a beer), a bread or a doughor a bread product, or a drink (e.g., a beer) or a beverage precursor(e.g., a wort). The food treatment processes of the invention can alsoinclude the use of any combination of other enzymes such astryptophanases or tyrosine decarboxylases, laccases, catalases,laccases, other cellulases, endoglycosidases, endo-beta-1,4-laccases,amyloglucosidases, other glucosidases, glucose isomerases,glycosyltransferases, lipases, phospholipases, lipooxygenases,beta-laccases, endo-beta-1,3(4)-laccases, cutinases, peroxidases,amylases, glucoamylases, pectinases, reductases, oxidases,decarboxylases, phenoloxidases, ligninases, pullulanases, arabinanases,hemicellulases, mannanases, xylolaccases, xylanases, pectin acetylesterases, rhamnogalacturonan acetyl esterases, proteases, peptidases,proteinases, polygalacturonases, rhamnogalacturonases, galactanases,pectin lyases, transglutaminases, pectin methylesterases,cellobiohydrolases, and/or glucose oxidases.

In one aspect, the invention provides enzymes and processes forhydrolyzing liquid (liquefied) and granular starch. Such starch can bederived from any source, e.g., beet, cane sugar, potato, corn, wheat,milo, sorghum, rye or bulgher. The invention applies to any plant starchsource, e.g., a grain starch source, which is useful in liquefaction(for example, to make biofuels comprising, e.g., a bioalcohol such asbioethanol, biomethanol, biobutanol or biopropanol), including any othergrain or vegetable source known to produce starch suitable forliquefaction. The methods of the invention comprise liquefying starch(e.g., making biofuels comprising, e.g., a bioalcohol such asbioethanol, biomethanol, biobutanol or biopropanol) from any naturalmaterial, such as rice, germinated rice, corn, barley, milo, wheat,legumes, potato, beet, cane sugar and sweet potato. The liquefyingprocess can substantially hydrolyze the starch to produce a syrup. Thetemperature range of the liquefaction can be any liquefactiontemperature which is known to be effective in liquefying starch. Forexample, the temperature of the starch can be between about 80° C. toabout 115° C., between about 100° C. to about 110° C., and from about105° C. to about 108° C. The bioalcohols made using the enzymes andprocesses of the invention can be used as fuels or in fuels (e.g., autofuels), e.g., as discussed below, in addition to their use in (or formaking) foods and feeds, including alcoholic beverages.

6.30. Waste Treatment

In alternative embodiments, the invention provides enzymes for use inwaste treatment. Enzymes of the invention can be used in a variety ofwaste treatment or related industrial applications, e.g., in wastetreatment related to biomass conversion to generate fuels. For example,in one aspect, the invention provides a solid and/or liquid wastedigestion process using the lignocellulosic enzyme of the invention. Themethods can comprise reducing the mass and volume of substantiallyuntreated solid waste. Solid waste can be treated with an enzymaticdigestive process in the presence of an enzymatic solution (includingthe lignocellulosic enzymes of the invention) at a controlledtemperature. This results in a reaction without appreciable bacterialfermentation from added microorganisms. The solid waste is convertedinto a liquefied waste and any residual solid waste. The resultingliquefied waste can be separated from said any residual solidifiedwaste. See e.g., U.S. Pat. No. 5,709,796. In one aspect, thecompositions and methods of the invention are used for odor removal,odor prevention or odor reduction, e.g., in animal waste lagoons, e.g.,on swine farms, in other agricultural, food or feed processing, inclothing and/or textile processing, cleaning or recycling, or otherindustrial processes.

In alternative embodiments, enzymes and methods for the conversion ofbiomass (e.g., lignocellulosic materials) to fuels (e.g., biofuelscomprising, e.g., a bioalcohol such as bioethanol, biomethanol,biobutanol or biopropanol) can incorporate the treatment/recycling ofmunicipal solid waste material, including waste obtained directly from amunicipality or municipal solid waste that was previously land-filledand subsequently recovered, or sewage sludge, e.g., in the form ofsewage sludge cake which contains substantial amounts of cellulosicmaterial. Since sewage sludge cakes will normally not containsubstantial amounts of recyclable materials (aluminum, glass, plastics,etc.), they can be directly treated with concentrated sulfuric acid (toreduce the heavy metal content of the cellulosic component of the waste)and processed in the ethanol production system. See, e.g., U.S. Pat.Nos. 6,267,309; 5,975,439.

Another exemplary method using enzymes of the invention for recoveringorganic and inorganic matter from waste material comprises sterilizing asolid organic matter and softening it by subjecting it to heat andpressure. This exemplary process may be carried out by first agitatingwaste material and then subjecting it to heat and pressure, whichsterilizes it and softens the organic matter contained therein. In oneaspect, after heating under pressure, the pressure may be suddenlyreleased from a perforated chamber to forces the softened organic matteroutwardly through perforations of the container, thus separating theorganic matter from the solid inorganic matter. The softened sterilized,organic matter is then fermented in fermentation chamber, e.g., usingenzymes of the invention, e.g., to form a mash. The mash may besubjected to further processing by centrifuge, distillation columnand/or anaerobic digester to recover fuels such as ethanol and methane,and animal feed supplements. See, e.g., U.S. Pat. No. 6,251,643.

Enzymes of the invention can also be used in processes, e.g.,pretreatments, to reduce the odor of an industrial waste, or a wastegenerated from an animal production facility, and the like. For example,enzymes of the invention can be used to treat an animal waste in a wasteholding facility to enhance efficient degradation of large amounts oforganic matter with reduced odor. The process can also includeinoculation with sulfide-utilizing bacteria and organic digestingbacteria and lytic enzymes (in addition to an enzyme of the invention).See, e.g., U.S. Pat. No. 5,958,758.

Enzymes of the invention can also be used in mobile systems, e.g., batchtype reactors, for bioremediation of aqueous, hazardous wastes, e.g., asdescribed in U.S. Pat. No. 5,833,857. Batch type reactors can be largevessels having circulatory capability wherein bacteria (e.g., expressingan enzyme of the invention) are maintained in an efficient state bynutrients being feed into the reactor. Such systems can be used whereeffluent can be delivered to the reactor or the reactor is built into awaste water treatment system. Enzymes of the invention can also be usedin treatment systems for use at small or temporary remote locations,e.g., portable, high volume, highly efficient, versatile waste watertreatment systems. The waste treatment processes of the invention caninclude the use of any combination of other enzymes such as other thelignocellulosic enzyme, e.g., glycosyl hydrolase, cellulase,endoglucanase, cellobiohydrolase, beta-glucosidase, xylanase, mannanse,β-xylosidase and/or arabinofuranosidase enzymes, catalases, laccases,other cellulases, endoglycosidases, endo-beta-1,4-laccases,amyloglucosidases, other glucosidases, glucose isomerases,glycosyltransferases, lipases, phospholipases, lipooxygenases,beta-laccases, endo-beta-1,3(4)-laccases, cutinases, peroxidases,amylases, glucoamylases, pectinases, reductases, oxidases,decarboxylases, phenoloxidases, ligninases, pullulanases, phytases,arabinanases, hemicellulases, mannanases, xylolaccases, xylanases,pectin acetyl esterases, rhamnogalacturonan acetyl esterases, proteases,peptidases, proteinases, polygalacturonases, rhamnogalacturonases,galactanases, pectin lyases, transglutaminases, pectin methylesterases,other cellobiohydrolases, and/or glucose oxidases.

6.31. Detergent Compositions

In alternative embodiments, the invention provides detergentcompositions comprising one or more polypeptides of the invention (e.g.,enzymes having cellulase or cellobiohydrolase activity) and methods ofmaking and using these compositions. The invention incorporates allmethods of making and using detergent compositions, see, e.g., U.S. Pat.No. 6,413,928; 6,399,561; 6,365,561; 6,380,147. The detergentcompositions can be a one and two part aqueous composition, anon-aqueous liquid composition, a cast solid, a granular form, aparticulate form, a compressed tablet, a gel and/or a paste and a slurryform. The invention also provides methods capable of a rapid removal ofgross food soils, films of food residue and other minor foodcompositions using these detergent compositions. Enzymes of theinvention can facilitate the removal of starchy stains by means ofcatalytic hydrolysis of the starch polysaccharide. Enzymes of theinvention can be used in dishwashing detergents in textile launderingdetergents.

The actual active enzyme content depends upon the method of manufactureof a detergent composition and is not critical, assuming the detergentsolution has the desired enzymatic activity. In one aspect, the amountof glucosidase present in the final solution ranges from about 0.001 mgto 0.5 mg per gram of the detergent composition. The particular enzymechosen for use in the process and products of this invention dependsupon the conditions of final utility, including the physical productform, use pH, use temperature, and soil types to be degraded or altered.The enzyme can be chosen to provide optimum activity and stability forany given set of utility conditions. In one aspect, the polypeptides ofthe present invention are active in the pH ranges of from about 4 toabout 12 and in the temperature range of from about 20° C. to about 95°C. The detergents of the invention can comprise cationic, semi-polarnonionic or zwitterionic surfactants; or, mixtures thereof.

Enzymes of the present invention can be formulated into powdered andliquid detergents having pH between 4.0 and 12.0 at levels of about 0.01to about 5% (preferably 0.1% to 0.5%) by weight. These detergentcompositions can also include other enzymes such as known proteases,cellulases, lipases or endoglycosidases, and/or glucose oxidases, aswell as builders and stabilizers. The addition of enzymes of theinvention to conventional cleaning compositions does not create anyspecial use limitation. In other words, any temperature and pH suitablefor the detergent is also suitable for the present compositions as longas the pH is within the above range, and the temperature is below thedescribed enzyme's denaturing temperature. In addition, the polypeptidesof the invention can be used in a cleaning composition withoutdetergents, again either alone or in combination with builders andstabilizers.

The present invention provides cleaning compositions including detergentcompositions for cleaning hard surfaces, detergent compositions forcleaning fabrics, dishwashing compositions, oral cleaning compositions,denture cleaning compositions, and contact lens cleaning solutions.

In one aspect, the invention provides a method for washing an objectcomprising contacting the object with a polypeptide of the inventionunder conditions sufficient for washing. A polypeptide of the inventionmay be included as a detergent additive. The detergent composition ofthe invention may, for example, be formulated as a hand or machinelaundry detergent composition comprising a polypeptide of the invention.A laundry additive suitable for pre-treatment of stained fabrics cancomprise a polypeptide of the invention. A fabric softener compositioncan comprise a polypeptide of the invention. Alternatively, apolypeptide of the invention can be formulated as a detergentcomposition for use in general household hard surface cleaningoperations.

In alternative aspects, detergent additives and detergent compositionsof the invention may comprise one or more other enzymes such as aprotease, a lipase, a cutinase, another glucosidase, a carbohydrase,another cellulase, a pectinase, a mannanase, an arabinase, agalactanase, a xylanase, an oxidase, e.g., a lactase, and/or aperoxidase, and/or glucose oxidase. The properties of the enzyme(s) ofthe invention are chosen to be compatible with the selected detergent(i.e. pH-optimum, compatibility with other enzymatic and non-enzymaticingredients, etc.) and the enzyme(s) is present in effective amounts. Inone aspect, enzymes of the invention are used to remove malodorousmaterials from fabrics. Various detergent compositions and methods formaking them that can be used in practicing the invention are describedin, e.g., U.S. Pat. Nos. 6,333,301; 6,329,333; 6,326,341; 6,297,038;6,309,871; 6,204,232; 6,197,070; 5,856,164.

In alternative embodiments, the detergents and related processes of theinvention can also include the use of any combination of other enzymessuch as tryptophanases or tyrosine decarboxylases, laccases, catalases,laccases, other cellulases, endoglycosidases, endo-beta-1,4-laccases,amyloglucosidases, other glucosidases, glucose isomerases,glycosyltransferases, lipases, phospholipases, lipooxygenases,beta-laccases, endo-beta-1,3(4)-laccases, cutinases, peroxidases,amylases, glucoamylases, pectinases, reductases, oxidases,decarboxylases, phenoloxidases, ligninases, pullulanases, arabinanases,hemicellulases, mannanases, xylolaccases, xylanases, pectin acetylesterases, rhamnogalacturonan acetyl esterases, proteases, peptidases,proteinases, polygalacturonases, rhamnogalacturonases, galactanases,pectin lyases, transglutaminases, pectin methylesterases, othercellobiohydrolases, and/or glucose oxidases.

6.32. Treating Fabrics and Textiles

In alternative embodiments, the invention provides methods of treatingfabrics and textiles using one or more polypeptides of the invention.The polypeptides of the invention can be used in any fabric-treatingmethod, which are well known in the art, see, e.g., U.S. Pat. No.6,077,316. For example, in one aspect, the feel and appearance of afabric is improved by a method comprising contacting the fabric with anenzyme of the invention in a solution. In one aspect, the fabric istreated with the solution under pressure.

In one aspect, the enzymes of the invention are applied during or afterthe weaving of textiles, or during the desizing stage, or one or moreadditional fabric processing steps. During the weaving of textiles, thethreads are exposed to considerable mechanical strain. Prior to weavingon mechanical looms, warp yarns are often coated with sizing starch orstarch derivatives in order to increase their tensile strength and toprevent breaking. The enzymes of the invention can be applied to removethese sizing starch or starch derivatives. After the textiles have beenwoven, a fabric can proceed to a desizing stage. This can be followed byone or more additional fabric processing steps. Desizing is the act ofremoving size from textiles. After weaving, the size coating must beremoved before further processing the fabric in order to ensure ahomogeneous and wash-proof result. The invention provides a method ofdesizing comprising enzymatic hydrolysis of the size by the action of anenzyme of the invention.

The enzymes of the invention can be used to desize fabrics, includingcotton-containing fabrics, as detergent additives, e.g., in aqueouscompositions. The invention provides methods for producing a stonewashedlook on indigo-dyed denim fabric and garments. For the manufacture ofclothes, the fabric can be cut and sewn into clothes or garments, whichis afterwards finished. In particular, for the manufacture of denimjeans, different enzymatic finishing methods have been developed. Thefinishing of denim garment normally is initiated with an enzymaticdesizing step, during which garments are subjected to the action ofamylolytic enzymes in order to provide softness to the fabric and makethe cotton more accessible to the subsequent enzymatic finishing steps.The invention provides methods of finishing denim garments (e.g., a“bio-stoning process”), enzymatic desizing and providing softness tofabrics using the Enzymes of the invention. The invention providesmethods for quickly softening denim garments in a desizing and/orfinishing process. The invention also provides disinfectants comprisingenzymes of the invention.

The fabric or textile treatment processes of the invention can alsoinclude the use of any combination of other enzymes such astryptophanases or tyrosine decarboxylases, laccases, catalases,laccases, other cellulases, endoglycosidases, endo-beta-1,4-laccases,amyloglucosidases, other glucosidases, glucose isomerases,glycosyltransferases, lipases, phospholipases, lipooxygenases,beta-laccases, endo-beta-1,3(4)-laccases, cutinases, peroxidases,amylases, glucoamylases, pectinases, reductases, oxidases,decarboxylases, phenoloxidases, ligninases, pullulanases, arabinanases,hemicellulases, mannanases, xylolaccases, xylanases, pectin acetylesterases, rhamnogalacturonan acetyl esterases, proteases, peptidases,proteinases, polygalacturonases, rhamnogalacturonases, galactanases,pectin lyases, transglutaminases, pectin methylesterases, othercellobiohydrolases, and/or glucose oxidases.

6.33. Paper or Pulp Treatment

In alternative embodiments, enzymes of the invention can be in paper orpulp treatment or paper deinking. For example, in one aspect, theinvention provides a paper treatment process using enzymes of theinvention. In one aspect, the enzymes of the invention can be used tomodify starch in the paper thereby converting it into a liquefied form.In another aspect, paper components of recycled photocopied paper duringchemical and enzymatic deinking processes. In alternative embodiments,enzymes of the invention can be used in combination with other enzymes,including other cellulases (including other endoglucanases,cellobiohydrolases and/or beta-glucosidases). The wood, wood waste,paper, paper product or pulp can be treated by the following threeprocesses: 1) disintegration in the presence of an enzyme of theinvention, 2) disintegration with a deinking chemical and an enzyme ofthe invention, and/or 3) disintegration after soaking with an enzyme ofthe invention. The recycled paper treated with an enzyme of theinvention can have a higher brightness due to removal of toner particlesas compared to the paper treated with just cellulase. While theinvention is not limited by any particular mechanism, the effect of anenzyme of the invention may be due to its behavior as surface-activeagents in pulp suspension.

In alternative embodiments, the invention provides methods of treatingpaper and paper pulp using one or more polypeptides of the invention.The polypeptides of the invention can be used in any paper- orpulp-treating method, which are well known in the art, see, e.g., U.S.Pat. Nos. 6,241,849; 6,066,233; 5,582,681. For example, in one aspect,the invention provides a method for deinking and decolorizing a printedpaper containing a dye, comprising pulping a printed paper to obtain apulp slurry, and dislodging an ink from the pulp slurry in the presenceof an enzyme of the invention (other enzymes can also be added). Inanother aspect, the invention provides a method for enhancing thefreeness of pulp, e.g., pulp made from secondary fiber, by adding anenzymatic mixture comprising an enzyme of the invention (can alsoinclude other enzymes, e.g., pectinase enzymes) to the pulp and treatingunder conditions to cause a reaction to produce an enzymatically treatedpulp. The freeness of the enzymatically treated pulp is increased fromthe initial freeness of the secondary fiber pulp without a loss inbrightness.

In alternative embodiments, the paper, wood, wood waste, or pulptreatment or recycling processes of the invention can also include theuse of any combination of other enzymes such as tryptophanases ortyrosine decarboxylases, laccases, catalases, laccases, othercellulases, endoglycosidases, endo-beta-1,4-laccases, amyloglucosidases,other glucosidases, glucose isomerases, glycosyltransferases, lipases,phospholipases, lipooxygenases, beta-laccases,endo-beta-1,3(4)-laccases, cutinases, peroxidases, amylases,glucoamylases, pectinases, reductases, oxidases, decarboxylases,phenoloxidases, ligninases, pullulanases, arabinanases, hemicellulases,mannanases, xylolaccases, xylanases, pectin acetyl esterases,rhamnogalacturonan acetyl esterases, proteases, peptidases, proteinases,polygalacturonases, rhamnogalacturonases, galactanases, pectin lyases,transglutaminases, pectin methylesterases, other cellobiohydrolases,and/or glucose oxidase.

6.34. Repulping: Treatment of Lignocellulosic Materials

In alternative embodiments, the invention also provides a method for thetreatment of lignocellulosic fibers, wherein the fibers are treated witha polypeptide of the invention, in an amount which is efficient forimproving the fiber properties. The enzymes of the invention may also beused in the production or recycling of lignocellulosic materials such aspulp, paper and cardboard, from starch reinforced waste paper andcardboard, especially where repulping or recycling occurs at pH above 7and where the enzymes of the invention can facilitate the disintegrationof the waste material through degradation of the reinforcing starch. Theenzymes of the invention can be useful in a process for producing apapermaking pulp from starch-coated printed paper. The process may beperformed as described in, e.g., WO 95/14807. An exemplary processcomprises disintegrating the paper to produce a pulp, treating with astarch-degrading enzyme before, during or after the disintegrating, andseparating ink particles from the pulp after disintegrating and enzymetreatment. See also U.S. Pat. No. 6,309,871 and other US patents citedherein. Thus, the invention includes a method for enzymatic deinking ofrecycled paper pulp, wherein the polypeptide is applied in an amountwhich is efficient for effective de-inking of the fiber surface.

6.35. Brewing and Fermenting

The invention provides methods of brewing (e.g., fermenting) beercomprising an enzyme of the invention. In one exemplary process,starch-containing raw materials are disintegrated and processed to forma malt. An enzyme of the invention is used at any point in thefermentation process. For example, enzymes of the invention can be usedin the processing of barley malt. The major raw material of beer brewingis barley malt. This can be a three stage process. First, the barleygrain can be steeped to increase water content, e.g., to around about40%. Second, the grain can be germinated by incubation at 15-25° C. for3 to 6 days when enzyme synthesis is stimulated under the control ofgibberellins. During this time enzyme levels rise significantly. In oneaspect, enzymes of the invention are added at this (or any other) stageof the process. The action of the enzyme results in an increase infermentable reducing sugars. This can be expressed as the diastaticpower, DP, which can rise from around 80 to 190 in 5 days at 12° C.

Enzymes of the invention can be used in any beer producing process, asdescribed, e.g., in U.S. Pat. Nos. 5,762,991; 5,536,650; 5,405,624;5,021,246; 4,788,066.

6.36. Increasing the Flow of Production Fluids from a SubterraneanFormation

In alternative embodiments, the invention provides methods for using anenzyme of the invention to increase the flow of production fluids from asubterranean formation by removing viscous, starch-containing, damagingfluids formed during production operations; these fluids can be foundwithin the subterranean formation which surrounds a completed well bore.In alternative embodiments, this results in production fluids being ableto flow from the well bore. This method of the invention also addressesthe problem of damaging fluids reducing the flow of production fluidsfrom a formation below expected flow rates.

In alternative embodiments, the invention provides for formulating anenzyme treatment (using an enzyme of the invention) by blending togetheran aqueous fluid and a polypeptide of the invention; pumping the enzymetreatment to a desired location within the well bore; allowing theenzyme treatment to degrade the viscous, starch-containing, damagingfluid, whereby the fluid can be removed from the subterranean formationto the well surface; and wherein the enzyme treatment is effective toattack the alpha glucosidic linkages in the starch-containing fluid.

In alternative embodiments, the subterranean formation enzyme treatmentprocesses of the invention can also include the use of any combinationof other enzymes such as tryptophanases or tyrosine decarboxylases,laccases, catalases, laccases, other cellulases, endoglycosidases,endo-beta-1,4-laccases, amyloglucosidases, other glucosidases, glucoseisomerases, glycosyltransferases, lipases, phospholipases,lipooxygenases, beta-laccases, endo-beta-1,3(4)-laccases, cutinases,peroxidases, amylases, glucoamylases, pectinases, reductases, oxidases,decarboxylases, phenoloxidases, ligninases, pullulanases, arabinanases,hemicellulases, mannanases, xylolaccases, xylanases, pectin acetylesterases, rhamnogalacturonan acetyl esterases, proteases, peptidases,proteinases, polygalacturonases, rhamnogalacturonases, galactanases,pectin lyases, transglutaminases, pectin methylesterases, othercellobiohydrolases, and/or glucose oxidase.

6.37. Pharmaceutical Compositions and Dietary Supplements

In alternative embodiments, the invention also provides pharmaceuticalcompositions and dietary supplements (e.g., dietary aids) comprising apolypeptide, e.g., a cellulase, of the invention. In alternativeembodiments, the cellulase activity comprises endoglucanase,cellobiohydrolase, beta-glucosidase, xylanase, mannanse, β-xylosidaseand/or arabinofuranosidase activity. In one aspect, the pharmaceuticalcompositions and dietary supplements (e.g., dietary aids) are formulatedfor oral ingestion, e.g., to improve the digestibility of foods andfeeds having a high cellulose or lignocellulosic component.

In alternative embodiments, periodontal treatment compounds can comprisean enzyme of the invention, e.g., as described in U.S. Pat. No.6,776,979. Compositions and methods for the treatment or prophylaxis ofacidic gut syndrome can comprise an enzyme of the invention, e.g., asdescribed in U.S. Pat. No. 6,468,964.

In alternative embodiments, wound dressings, implants and the likecomprise antimicrobial (e.g., antibiotic-acting) enzymes, including anenzyme of the invention (including, e.g., exemplary sequences of theinvention). Enzymes of the invention can also be used in alginatedressings, antimicrobial barrier dressings, burn dressings, compressionbandages, diagnostic tools, gel dressings, hydro-selective dressings,hydrocellular (foam) dressings, hydrocolloid dressings, I.V dressings,incise drapes, low adherent dressings, odor absorbing dressings, pastebandages, post operative dressings, scar management, skin care,transparent film dressings and/or wound closure. Enzymes of theinvention can be used in wound cleansing, wound bed preparation, totreat pressure ulcers, leg ulcers, burns, diabetic foot ulcers, scars,IV fixation, surgical wounds and minor wounds. Enzymes of the inventioncan be used to in sterile enzymatic debriding compositions, e.g.,ointments. In various aspects, the cellulase is formulated as a tablet,gel, pill, implant, liquid, spray, powder, food, feed pellet or as anencapsulated formulation.

6.38. Biodefense Applications

In other aspects, polypeptides, enzymes and antibodies of thisinvention, including enzymes having lignocellulosic activity, includingpolypeptides having cellulase or cellobiohydrolase activity, can be usedin biodefense; e.g., for the destruction of spores or microorganisms,e.g., bacteria, fungi, yeast, etc., comprising a lignocellulosicmaterial or any biologic polymer susceptible to hydrolysis by apolypeptide of this invention. Use of enzymes and antibodies of thisinvention, including enzymes having lignocellulosic activity, inbiodefense applications offers a significant benefit, in that they canbe very rapidly manufactured and/or developed against any currentlyunknown or biological warfare agents of the future. In addition, enzymeshaving lignocellulosic activity, including polypeptides havingcellulase, etc. activity, can be used for decontamination of affectedenvironments or materials, including clothing, or individuals. Thus, inaspect, the invention provides a biodefense or bio-detoxifying agent(s),or disinfecting agent, comprising a polypeptide having lignocellulosicactivity, including polypeptides having cellulase, etc. activity,wherein the polypeptide comprises a sequence of the invention(including, e.g., exemplary sequences of the invention), or apolypeptide encoded by a nucleic acid of the invention (including, e.g.,exemplary sequences of the invention), and methods of making and usingthem.

7. EXAMPLES Example 1

This example describes an exemplary protocol for the genetic engineeringof an enzyme of the invention. The engineered, or “optimized”, enzyme ofthe invention can be used in the conversion of biomass (e.g., bagasse)to monosaccharides, fuels and/or chemicals or other useful products;e.g., for making effective and sustainable alternatives topetroleum-based products. The engineered, or “optimized”, enzyme of theinvention can be expressed in organisms (e.g., microorganisms, such asbacteria or fungi) for its participation in chemical cycles involvingnatural biomass conversion. In one aspect, this engineered, or“optimized”, enzyme of the invention is used in “enzyme ensembles” forthe efficient depolymerization of cellulosic and hemicellulosic polymersto metabolizable carbon moieties. As discussed above, the inventionprovides methods for discovering and implementing the most effective ofenzymes to enable these important new “biomass conversion” andalternative energy industrial processes. Evolution technologies, forexample, Gene Site Saturation Mutagenesis (or GSSM) technology (asdiscussed above, see also U.S. Pat. Nos. 6,171,820 and 6,579,258),GeneReassembly technology (as discussed above, see also, e.g., U.S. Pat.No. 6,537,776), or Tailored Multi-Site Combinatorial Assembly^(SM)(TMCA^(SM)) technology (as discussed above, see also, e.g. PCTPublication Number WO 2009/018449), can be used for the discovery andoptimization of an enzyme component for lignocellulosic biomass material(e.g., cellulose) reduction (e.g., hydrolysis) to monosaccharides (e.g.,glucose), cellobiohydrolase and other carbohydrates.

In one embodiment, an enzyme discovery screen can be implemented usingVerenium Corporation's GIGAMATRIX® high throughput expression screeningplatform (discussed above) to identify enzymes, for example, to identifycellobiohydrolases using methylumbelliferyl cellobioside,methylumbelliferyl lactoside (MUL), phosphoric acid swollen cellulose(PASC), or bagasse (e.g., pretreated bagasse) as a substrate.

In one aspect, an enzyme can be chosen as a candidate for optimizationusing Gene Site Saturation Mutagenesis (or GSSM) technology. In oneembodiment, before performing GSSM evolution, the signal sequence, ifpresent, can be removed and a starting methionine added. As discussedabove, GSSM technology can rapidly mutate all amino acids in the proteinto the 19 other amino acids in a sequential fashion. Mutants can bescreened using a fiber-based assay and potential upmutants representingsingle amino acid changes can be identified. These upmutants can becombined into a new library representing combinations of the upmutants.This library can be screened resulting in identification of severalcandidate enzymes for commercialization.

Using GeneReassembly technology or Tailored Multi-Site CombinatorialAssembly technology, GSSM upmutants (enzyme-encoding sequence variants)can be “blended” (mixed together to achieve an optimal result) in orderto construct an enzyme with a desired activity or trait. The resultingenzymes can then be screened to identify candidate(s) with the bestdesired activity or trait (e.g., thermotolerance).

Example 2

Variant CBHI enzymes of the invention were made using GSSM technology(described above), see e.g. variants in Tables 1 and 3, were made usingSEQ ID NO:134 (encoded by SEQ ID NO:133) as the wild-type (parent). Theparent gene was inserted into the pDC-A2 vector and the variants weremade using GSSM technology. The library was transformed into E. coliStbl2, sequenced, and then passed on for fungal transformations intoAspergillus niger.

Entry Site variants, as well as Point Mutant Recombination variants, ofthe invention (see e.g. variants in Table 5), were made by combiningindividual mutations using Tailored Multi-Site Combinatorial Assemble(described above). The parent gene was inserted into the pDC-A2 vectorand the variants were made using GSSM technology. The library wastransformed into E. coli Stbl2, sequenced, and then passed on for fungaltransformations into Aspergillus niger.

CBHI variants of the invention in the Loop GeneReassembly library (seeTable 5) were made using GeneReassembly technology (described above),with the variants generated through “liquid ligation” of PCR productsand/or oligos followed by ligation into the pDC-A2 vector. This librarywas transformed into E. coli XL1-Blue, sequenced and then passed on forfungal transformations into Aspergillus niger.

The pDC-A2 vector used in making the CBH variants of the invention was areconstruction of the vector pGBFin-5 (described, e.g., in U.S. Pat. No.7,220,542), which was remade to reduce the total size of the vector. The2.1 kb 3′ Gla region of pGBFin-5 was reduced to 0.54 kb, the gpdpromoter remained the same, but the 2.24 kb amdS sequence was replacedby the 1.02 kb hygB gene encoding hygromycin phosphotransferase. The 2.3kb 3′ Gla region of pGBFin-5 was reduced to a 1.1 kb fragmentrepresenting the 5′ end of the original sequence. The E. coli repliconfor pDC-A2 was taken from pUC 18.

After transformation of the vector into E. coli Stbl2 or E. coliXL1-Blue, individual E. coli transformants were picked into 96-wellplates and grown in liquid culture in 200 μl LB plus ampicillin (100μg/ml) per well overnight at 30° C. The cells were then used to generatetemplate for sequencing reactions by colony PCR. The sequence data fromthe library of clones was analyzed to identify unique variants of CBHI.The E. coli transformants containing the selected variants were thenrearrayed in 96-well format and used to prepare linear DNA of the entireexpression cassette (the contents of pDC-A2 with the exception of the E.coli replicon) by PCR, using primers hybridizing to the ends of the 3′and 3″ Gla regions. Approximately 1 μg of PCR product from each clonewas then used to transform A. niger protoplasts in a PEG-mediatedtransformation in one well of a 96-well plate (i.e. one clone per well).Transformants were selected on regeneration agar (200 μl per well of PDAplus sucrose at 340 g/l and hygromycin at 200 μg/ml) in the same 96-wellformat. After 7 days incubation at 30° C., transformants were replicatedto 96-well plates containing PDA plus hygromycin (200 μg/ml) using apintool. Following incubation at 30° C. for a further 7 days, sporesfrom each well were used to inoculate 200 μl liquid media per well of a96-well plate. The plates were incubated at 30° C. for 7 days, and thesupernatant from each well, containing the secreted CBH variant, wasrecovered.

The media used to grow the Aspergillus transformed with expressionconstructs containing the variants had the following composition: NaNO₃,3.0 g/l; KCl, 0.26 g/l; KH₂PO₄, 0.76 g/l; 4M KOH, 0.56 ml/l; D-Glucose,5.0 g/l; Casamino Acids, 0.5 g/l; Trace Element Solution 0.5 ml/l;Vitamin Solution 5 ml/l; Penicillin-Streptomycin Solution (10,000 U/mland 10,000 μg/ml respectively) 5.0 ml/l; Maltose, 66.0 g/l; Soytone,26.4 g/l; (NH₄)₂50₄, 6.6 g/l; NaH₂PO₄.H₂O, 0.44 g/l; Mg50₄.7H₂O, 0.44g/l; Arginine, 0.44 g/l; Tween-80, 0.035 ml/l; Pleuronic Acid Antifoam,0.0088 ml/l; MES, 18.0 g/l. The Trace Element Solution had the followingcomposition in 100 ml: ZnSO₄.7H₂O, 2.2 g; H₃BO₃, 1.1 g; FeSO₄.7H₂O, 0.5g; CoCl₂.6H₂O, 0.17 g; CuSO₄.5H₂O, 0.16; MnCl₂.4H₂O, 0.5 g/l;NaMoO₄.2H₂O, 0.15 g/l; EDTA, 5 g/l. The Vitamin Solution had thefollowing composition in 500 ml: Riboflavin, 100 mg; Thiamine HCl, 100mg; Nicotinamide, 100 mg; Pyridoxine.HCl, 50 mg; Panthotenic Acid, 10mg; Biotin 0.2 mg.

Example 3

CBHI variants shown in Tables 1 and 5 were assayed under the followingconditions:

-   5% w/v pretreated bagasse (62.07% cellulose)-   35° C., 300 rpm shaking with 2 BBs per r×n-   pH5.2-   1 mM Sodium Azide-   5 ml total volume-   Enzyme Dosing Overview:

Enzyme Ratio CBHI 4 mg/g cellulose CBHII 2 mg/g cellulose EG 4 mg/gcellulose

-   Time point: T=0, 48 hours-   Time point (for Point Mutant Recombinants): T=0, 72 hours-   % improvement over wt=(% conversion of variant−% conversion of wt)/-   % conversion of wt    Results of these assays are shown in Tables 2 and 6.    -   CBHI variants shown in Table 3 were assayed under the following        conditions:

Samples heat challenged at 22 C, 60 C, 65 C, 70 C, 75 C, and 80 C for 20minutes. After heat challenge, samples cooled on ice. Residual activitydetermined on MUL at 22 C.

Calculations for % residual activity:% Residual Activity=Activity heat challenged sample/Activitynon-challenged sample  (22 C).All residual activities calculated indepentyl from parent residualactivity Melting Temperatures were determined by Differential Scanningcalorimetry, using 500-700 μg/mL of degassed sample.Results of these assays are shown in Table 4.

Example 4

The parent (wild-type) CBHI (SEQ ID NO:134, encoded by SEQ ID NO:133)and variant CBHI (SEQ ID NO:136, encoded by SEQ ID NO:135) were assayedto determine their cellobiose (product) inhibition.

In one assy, cellobiose inhibition was measured using methylumbelliferyllactoside (MUL) as the substrate. IC₅₀, the half maximal inhibitoryconcentration of cellobiose, was determined. The wild-type CBHI (SEQ IDNO:134) had an IC₅₀ of 0.06 g/L, while the CBHI mutant (SEQ ID NO:136)showed no inhibition up to 0.25 g/L cellobiose.

In another assay, cellobiose inhibition was measured using 0.1%phosphoric acid swollen cellulose (PASC) as the substrate. CBHI wasincubated with PASC and Calcofluor (which intercalates between cellulosestrands and fluoresces upon binding to cellulose) for 2 hours at 35° C.IC₅₀ was measured. The wild-type CBHI (SEQ ID NO:134) had an IC₅₀ of 2.2g/L, while the CBHI mutant (SEQ ID NO:136) showed no inhibition up to 25g/L cellobiose.

In another assay, cellobiose inhibition was measured in saccharificationassays using bagasse (12% solids in 200 mM MES buffer, pH 6) as thesubstrate. 5% w/v pretreated bagasse was incubated with 4 mg/g of CBHIat 35° C. at 20 RPM in hybridization ovens. Although the activity of thewild-type CBHI (SEQ ID NO:134) was higher than that of the CBHI mutant(SEQ ID NO:136), the activity of the mutant was less affected by thepresence of cellobiose (under either when no beta-glucosidase was addedor when gluconolactone was added). At 48 hours, wild-type CBHI activitydecreased by 60% when no beta-glucosidase was added, whereas theactivity of the CBHI mutant only decreased by 22% when beta-glucosidasewas added. At 72 hours, wild-type CBHI activity decreased by 50% whenbeta-glucosidase was added, whereas the activity of the CBHI mutant onlydecreased by 14% when beta-glucosidase was added.

A number of embodiments as provided herein have been described.Nevertheless, it will be understood that various modifications may bemade without departing from the spirit and scope as provided herein.Accordingly, other embodiments are within the scope of the claims.

TABLE 1 Muta- Plate tion Mutant Name Well Type Property NucleotideSequence AA Sequence 119484 B7 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 1, 2CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCCATACTGGACTTGGC WTPKSNNANTGLGNHGACAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCAT CCAELDIWEANSISEALTPCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCA HPCDTPGLSVCTTDACGGCTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTG TYSSDRYAGTCDPDGCDFCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCT NPYRLGVTDFYGSGKTVDACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCA TTKPITVVTQFVTDDGTSATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGT TGTLSEIRRYYVQNGVVIPTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCG QPSSKISGVSGNVINSDFCGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCAC DAEISTFGETASFSKHGGLCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGC AKMGAGMEAGMVLVMSGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACT LWDDYSVNMLWLDSTYPCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTAC TNATGTPGAARGSCPTTSCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACC GDPKTVESQSGSSYVTFSGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTG DIRVGPFNSTFSGGSSTGGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCAC SSTTTASGTTTTKASSTSTTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCC SSTSTGTGVAAHWGQCGAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCC GQGWTGPTTCASGTTCTAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGT VVNPYYSQCLGAACCCTTACTACTCTCAATGTTTGTAA 119484 H8 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 3, 4CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCGAGACTGGACTTGGC WTPSSNNAETGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 119483 H2 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 5, 6CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCAAGTCCAACAACGCCAACACTGGACTTGG WTPKSNNANTGLGNHGACAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCAT CCAELDIWEANSISEALTPCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCA HPCDTPGLSVCTTDACGGCTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTG TYSSDRYAGTCDPDGCDFCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCT NPYRLGVTDFYGSGKTVDACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCA TTKPITVVTQFVTDDGTSATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGT TGTLSEIRRYYVQNGVVIPTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCG QPSSKISGVSGNVINSDFCGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCAC DAEISTFGETASFSKHGGLCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGC AKMGAGMEAGMVLVMSGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACT LWDDYSVNMLWLDSTYPCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTAC TNATGTPGAARGSCPTTSCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACC GDPKTVESQSGSSYVTFSGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTG DIRVGPFNSTFSGGSSTGGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCAC SSTTTASGTTTTKASSTSTTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCC SSTSTGTGVAAHWGQCGAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCC GQGWTGPTTCASGTTCTAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGT VVNPYYSQCLGAACCCTTACTACTCTCAATGTTTGTAA 119498 A1 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 7, 8CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGATATGGC WTPSSNNANTGYGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 119498 C1 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 9, 10CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGAGTGGGC WTPSSNNANTGVGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 120175 D8 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 11, 12CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAASWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTTCGTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 120177 B4 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 13, 14CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPKTCASGTTCT GTTGGACTGGTCCTAAGACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 131921 A2 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 15, 16CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCCTT STNCYTGNTWNTAICLTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 132325 G11 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 17, 18CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCATTCTATCTGTTTGCACTHPCDTPILSVCTTDACGGT ACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGYSSDRYAGTCDPDGCDFN ACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACPYRLGVTDFYGSGKTVDT GGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTKPITVVTQFVTDDGTST TCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTAGTLSEIRRYYVQNGVVIP CTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAQPSSKISGVSGNVINSDFC GTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTDAEISTFGETASFSKHGGL TTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCAKMGAGMEAGMVLVMS TGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCCLWDDYSVNMLWLDSTYP GTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCCTNATGTPGAARGSCPTTS CCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGTGDPKTVESQSGSSYVTFS TGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 131900 C9 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 19, 20CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCG LLNQEFTFTVDVSGLPCGGGCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGA LNGALYFVTMDADGGVSCGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTT KYPNNKAGAQYGVGYCDGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGG SQCPRDLKFIAGQANVEGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGG WTPSSNNANTGLGNHGACAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCAT CCAELDIWEANSISEALTPCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCA HPCDTPGLSVCTTDACGGCTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTG TYSSDRYAGTCDPDGCDFCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCT NPYRLGVTDFYGSGKTVDACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCA TTKPITVVTQFVTDDGTSATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGT TGTLSEIRRYYVQNGVVIPTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCG QPSSKISGVSGNVINSDFCGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCAC DAEISTFGETASFSKHGGLCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGC AKMGAGMEAGMVLVMSGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACT LWDDYSVNMLWLDSTYPCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTAC TNATGTPGAARGSCPTTSCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACC GDPKTVESQSGSSYVTFSGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTG DIRVGPFNSTFSGGSSTGGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCAC SSTTTASGTTTTKASSTSTTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCC SSTSTGTGVAAHWGQCGAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCC GQGWTGPTTCASGTTCTAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGT VVNPYYSQCLGAACCCTTACTACTCTCAATGTTTGTAA 131901 G9 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 21, 22CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLGCGCCTCGGGTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 131909 G8 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 23, 24CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACGCTAAGGCCGGCGCTCAGTACGGTGTTG KYPNAKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 131900 A2 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 25, 26CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCGGTC LLNQEFTFTVDVGHLPCGACCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGA LNGALYFVTMDADGGVSCGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTT KYPNNKAGAQYGVGYCDGGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGG SQCPRDLKFIAGQANVEGCCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGG WTPSSNNANTGLGNHGACAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCAT CCAELDIWEANSISEALTPCTCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCA HPCDTPGLSVCTTDACGGCTACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTG TYSSDRYAGTCDPDGCDFCGACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCT NPYRLGVTDFYGSGKTVDACGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCA TTKPITVVTQFVTDDGTSATTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGT TGTLSEIRRYYVQNGVVIPTACTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCG QPSSKISGVSGNVINSDFCGAGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCAC DAEISTFGETASFSKHGGLCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGC AKMGAGMEAGMVLVMSGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACT LWDDYSVNMLWLDSTYPCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTAC TNATGTPGAARGSCPTTSCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACC GDPKTVESQSGSSYVTFSGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTG DIRVGPFNSTFSGGSSTGGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCAC SSTTTASGTTTTKASSTSTTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCC SSTSTGTGVAAHWGQCGAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCC GQGWTGPTTCASGTTCTAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGT VVNPYYSQCLGAACCCTTACTACTCTCAATGTTTGTAA 132821 H1 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 27, 28CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCCCCAACAACGCCAACACTGGACTTGGC WTPSPNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVSDDGTSTTCGTCTCTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA GTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 132821 F9 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 29, 30CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDQGTSSTCGTCACTGACCAGGGCACATCCTCCGGCACCCTCTCCGAGATCAGACGTTA GTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGGTCTCCACCT DAEVSTFGETASFSKHGGTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC LAKMGAGMEAGMVLVMTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC SLWDDYSVNMLWLDSTYGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC PTNATGTPGAARGSCPTTCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT SGDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 132824 G7 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 31, 32CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCCGTCTCTCCGAGATCAGACGTTA TGRLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 132825 B2 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 33, 34CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCCTTGAGATCAGACGTTA TGTLLEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 132828 G11 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 35, 36CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVSNGVVIPCTACGTTAGTAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 132832 G9 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 37, 38CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCGATATCTCCGGA QPSSDISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 132834 G4 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 39, 40CATCCCTCTTTGAGCTGGTCTACTTGCAGATCGGGTGGTAGCTGCACCACAA PSLSWSTCRSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCGCTGACTTCTAC NPYRLGVADFYGSGKTVGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT DTTKPITVVTQFVTDDGTTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA STGTLSEIRRYYVQNGVVICTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA PQPSSKISGVCGNVINSDFGTCTGTGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT CDAEISTFGETASFSKHGGTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC LAKMGAGMEAGMVLVMTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC SLWDDYSVNMLWLDSTYGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC PTNATGTPGAARGSCPTTCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT SGDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 132834 H7 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 41, 42CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSDNVINSDFCGTCAGCGATAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 132835 G5 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 43, 44CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGVVINSDFCGTCAGCGGAGTTGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 132836 H7 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 45, 46CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDLCGTCAGCGGAAATGTCATCAACTCCGACTTGTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 133543 H4 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 47, 48CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETISFSKHGGLTTGGCGAGACTATTTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 133544 H2 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 49, 50CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHRGLTTGGCGAGACTGCCTCCTTCAGCAAACACCGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 133547 G11 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 51, 52CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMSAGMVLVMSTGGTATGAGTGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 133562 H4 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 53, 54CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGTGGGGT DIRWGPFNSTFSGGSSTGGCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTA SSTTTASGTTTTKASSTSTCTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAG SSTSTGTGVAAHWGQCGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAG GQGWTGPTTCASGTTCTGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGA VVNPYYSQCLACCCTTACTACTCTCAATGTTTGTAA 133694 B3 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 55, 56CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFGSTFSGGSSTGG CTTTCGGTTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA 133696 D5 GSSM Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 57, 58CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSKTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAAGACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA Parent Activity-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTC MSALNSFNMYKSALILGSSEQ ID CTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCLLATAGAQQIGTYTAETH NO: 59, 60CATCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAA PSLSWSTCKSGGSCTTNSACTCCGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAA GAITLDANWRWVHGVNTTACCAGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGAC STNCYTGNTWNTAICDTDACTGATGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTG ASCAQDCALDGADYSGTGCACGTACGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTAC YGITTSGNSLRLNFVTGSNCGGTTCCAACGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTAC VGSRTYLMADNTHYQIFDCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCA LLNQEFTFTVDVSHLPCGCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGAC LNGALYFVTMDADGGVSGGTGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTG KYPNNKAGAQYGVGYCDGATACTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGC SQCPRDLKFIAGQANVEGCAACGTTGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGC WTPSSNNANTGLGNHGAAACCACGGAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCT CCAELDIWEANSISEALTPCAGAGGCTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACT HPCDTPGLSVCTTDACGGACTGATGCCTGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCG TYSSDRYAGTCDPDGCDFACCCTGATGGATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTAC NPYRLGVTDFYGSGKTVDGGCTCCGGCAAGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAAT TTKPITVVTQFVTDDGTSTCGTCACTGACGACGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTA TGTLSEIRRYYVQNGVVIPCTACGTTCAGAACGGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGA QPSSKISGVSGNVINSDFCGTCAGCGGAAATGTCATCAACTCCGACTTCTGCGATGCTGAGATCTCCACCT DAEISTFGETASFSKHGGLTTGGCGAGACTGCCTCCTTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGC AKMGAGMEAGMVLVMSTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGTTTGTGGGACGACTACTCC LWDDYSVNMLWLDSTYPGTCAACATGCTCTGGCTCGACAGCACCTACCCTACAAACGCGACTGGTACCC TNATGTPGAARGSCPTTSCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGGGACCCTAAGACCGT GDPKTVESQSGSSYVTFSTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGACATCCGGGTTGGTCDIRVGPFNSTFSGGSSTGG CTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGCAGCTCCACTACSSTTTASGTTTTKASSTST TACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTCTACTTCCAGCSSTSTGTGVAAHWGQCG ACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTGGTGGCCAGGGQGWTGPTTCASGTTCT GTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACCGTCGTGAAVVNPYYSQCL CCCTTACTACTCTCAATGTTTGTAA

TABLE 2 Mutation % improvement Dose Plate Name Well Type Mutant Propertyover WT @ 48 hr Reduction 119484 B7 GSSM Activity-SEQ ID NO: 1, 2 12.3%119484 H8 GSSM Activity-SEQ ID NO: 3, 4  7.2% 119483 H2 GSSMActivity-SEQ ID NO: 5, 6 13.0% 119498 A1 GSSM Activity-SEQ ID NO: 7, 811.4% 0.75X 119498 C1 GSSM Activity-SEQ ID NO: 9, 10 13.3% 0.75X 120175D8 GSSM Activity-SEQ ID NO: 11, 12  0.0% 0.94X 120177 B4 GSSMActivity-SEQ ID NO: 13, 14  0.0% 0.87X 131921 A2 GSSM Activity-SEQ IDNO: 15, 16  1.0% 132325 G11 GSSM Activity-SEQ ID NO: 17, 18  2.3% 0.75X131900 C9 GSSM Activity-SEQ ID NO: 19, 20  8.8% 0.75X 131901 G9 GSSMActivity-SEQ ID NO: 21, 22 11.0% 0.75X 131909 G8 GSSM Activity-SEQ IDNO: 23, 24  0.9% 0.75X 131900 A2 GSSM Activity-SEQ ID NO25, 26  5.8%0.75X 132821 H1 GSSM Activity-SEQ ID NO: 27, 28  2.9% 0.75X 132821 F9GSSM Activity-SEQ ID NO: 29, 30 13.9% 0.75X 132824 G7 GSSM Activity-SEQID NO: 31, 32 11.1% 0.75X 132825 B2 GSSM Activity-SEQ ID NO: 33, 3413.4% 0.75X 132828 G11 GSSM Activity-SEQ ID NO: 35, 36  7.5% 0.75X132832 G9 GSSM Activity-SEQ ID NO: 37, 38  6.9% 0.75X 132834 G4 GSSMActivity-SEQ ID NO: 39, 40  4.0%   1X 132834 H7 GSSM Activity-SEQ ID NO:41, 42  3.8%   1X 132835 G5 GSSM Activity-SEQ ID NO: 43, 44  8.7% 0.75X132836 H7 GSSM Activity-SEQ ID NO: 45, 46  3.9% 0.75X 133543 H4 GSSMActivity-SEQ ID NO: 47, 48  4.8%   1X 133544 H2 GSSM Activity-SEQ ID NO:49, 50  1.7%   1X 133547 G11 GSSM Activity-SEQ ID NO: 51, 52  7.7% 0.75X133562 H4 GSSM Activity-SEQ ID NO: 53, 54  8.7% 0.75X 133694 B3 GSSMActivity-SEQ ID NO: 55, 56  0.8%   1X 133696 D5 GSSM Activity-SEQ ID NO:57, 58  1.1% Parent Activity-SEQ ID NO: 59, 60  0.0%

TABLE 3 Plate Mutation Mutant Name Well Type Property NucleotideSequence AA Sequence 131175 B1 GSSM Thermo-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS toleranceTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCA LLATAGAQQIGTYTAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNS 61, 62CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA GAITLDANWRWVHGVNGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TSTNCYTGNTWNTAICDGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACAATGGCACGTA TDASCAQDCALDGADYNCGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAAGTYGITTSGNSLRLNFVT CGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGGSNVGSRTYLMADNTHY ACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGQIFDLLNQEFTFTVDVSH GTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCLPCGLNGALYFVTMDAD AAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCGGVSKYPNNKAGAQYG TCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTVGYCDSQCPRDLKFIAGQ GGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCANVEGWTPSSNNANTGL TGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCGNHGACCAELDIWEANSITCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGSEALTPHPCDTPGLSVCTTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTT TDACGGTYSSDRYAGTCCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGA DPDGCDFNPYRLGVTDFCACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACAT YGSGKTVDTTKPITVVTQCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTC FVTDDGTSTGTLSEIRRYATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCYVQNGVVIPQPSSKISGVGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAASGNVINSDFCDAEISTFGECACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGT TASFSKHGGLAKMGAGCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCT MEAGMVLVMSLWDDYSACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACC VNMLWLDSTYPTNATGTACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAC PGAARGSCPTTSGDPKTVCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGESQSGSSYVTFSDIRVGPFCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCT NSTFSGGSSTGGSSTTTACTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGSGTTTTKASSTSTSSTSTGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACC TGVAAHWGQCGGQGWTACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA GPTTCASGTTCTVVNPY YSQCL132309 B7 GSSM Thermo-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS toleranceTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCA LLATAGAQQIGTYTAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNS 63, 64CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA GAITLDANWRWVHGVNGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TSTNCYTGNTWNTAICDGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTAC TDASCAQDCALDGADYSGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCAGTACCGGTTCCAACGTYGITTSGNSLRLNFST GTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGAGSNVGSRTYLMADNTHY CTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGQIFDLLNQEFTFTVDVSH TTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCALPCGLNGALYFVTMDAD AGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTGGVSKYPNNKAGAQYG CAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGVGYCDSQCPRDLKFIAGQ GACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTANVEGWTPSSNNANTGL GCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTGNHGACCAELDIWEANSICACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTSEALTPHPCDTPGLSVCT ACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTTDACGGTYSSDRYAGTC CAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGADPDGCDFNPYRLGVTDF CACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATYGSGKTVDTTKPITVVTQ CCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCFVTDDGTSTGTLSEIRRYATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCYVQNGVVIPQPSSKISGVGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAASGNVINSDFCDAEISTFGECACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGT TASFSKHGGLAKMGAGCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCT MEAGMVLVMSLWDDYSACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACC VNMLWLDSTYPTNATGTACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAC PGAARGSCPTTSGDPKTVCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGESQSGSSYVTFSDIRVGPFCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCT NSTFSGGSSTGGSSTTTACTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGSGTTTTKASSTSTSSTSTGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACC TGVAAHWGQCGGQGWTACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA GPTTCASGTTCTVVNPY YSQCL132309 H7 GSSM Thermo-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS toleranceTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCA LLATAGAQQIGTYTAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNS 65, 66CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA GAITLDANWRWVHGVNGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TSTNCYTGNTWNTAICDGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTAC TDASCAQDCALDGADYSGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCACTACCGGTTCCAACGTYGITTSGNSLRLNFTT GTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGAGSNVGSRTYLMADNTHY CTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGQIFDLLNQEFTFTVDVSH TTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCALPCGLNGALYFVTMDAD AGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTGGVSKYPNNKAGAQYG CAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGVGYCDSQCPRDLKFIAGQ GACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTANVEGWTPSSNNANTGL GCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTGNHGACCAELDIWEANSICACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTSEALTPHPCDTPGLSVCT ACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTTDACGGTYSSDRYAGTC CAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGADPDGCDFNPYRLGVTDF CACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATYGSGKTVDTTKPITVVTQ CCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCFVTDDGTSTGTLSEIRRYATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCYVQNGVVIPQPSSKISGVGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAASGNVINSDFCDAEISTFGECACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGT TASFSKHGGLAKMGAGCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCT MEAGMVLVMSLWDDYSACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACC VNMLWLDSTYPTNATGTACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAC PGAARGSCPTTSGDPKTVCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGESQSGSSYVTFSDIRVGPFCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCT NSTFSGGSSTGGSSTTTACTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGSGTTTTKASSTSTSSTSTGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACC TGVAAHWGQCGGQGWTACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA GPTTCASGTTCTVVNPY YSQCL131179 G5 GSSM Thermo-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS toleranceTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCA LLATAGAQQIGTYTAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNS 67, 68CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA GAITLDANWRWVHGVNGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TSTNCYTGNTWNTAICDGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTAC TDASCAQDCALDGADYSGGTATCACTACCTCCAATAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTYGITTSNNSLRLNFVT GTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGAGSNVGSRTYLMADNTHY CTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGQIFDLLNQEFTFTVDVSH TTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCALPCGLNGALYFVTMDAD AGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTGGVSKYPNNKAGAQYG CAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGVGYCDSQCPRDLKFIAGQ GACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTANVEGWTPSSNNANTGL GCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTGNHGACCAELDIWEANSICACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTSEALTPHPCDTPGLSVCT ACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTTDACGGTYSSDRYAGTC CAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGADPDGCDFNPYRLGVTDF CACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATYGSGKTVDTTKPITVVTQ CCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCFVTDDGTSTGTLSEIRRYATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCYVQNGVVIPQPSSKISGVGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAASGNVINSDFCDAEISTFGECACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGT TASFSKHGGLAKMGAGCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCT MEAGMVLVMSLWDDYSACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACC VNMLWLDSTYPTNATGTACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAC PGAARGSCPTTSGDPKTVCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGESQSGSSYVTFSDIRVGPFCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCT NSTFSGGSSTGGSSTTTACTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGSGTTTTKASSTSTSSTSTGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACC TGVAAHWGQCGGQGWTACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA GPTTCASGTTCTVVNPY YSQCL131180 D10 GSSM Thermo-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS toleranceTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCA LLATAGAQQIGTYTAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNS 69, 70CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA GAITLDANWRWVHGVNGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TSTNCYTGNTWNTAICDGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTAC TDASCAQDCALDGADYSGGTATCACTACCTCCGGCAACTCAACGCGCCTGAACTTCGTTACCGGTTCCAACGTYGITTSGNSTRLNFVT GTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGAGSNVGSRTYLMADNTHY CTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGQIFDLLNQEFTFTVDVSH TTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCALPCGLNGALYFVTMDAD AGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTGGVSKYPNNKAGAQYG CAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGVGYCDSQCPRDLKFIAGQ GACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTANVEGWTPSSNNANTGL GCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTGNHGACCAELDIWEANSICACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTSEALTPHPCDTPGLSVCT ACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTTDACGGTYSSDRYAGTC CAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGADPDGCDFNPYRLGVTDF CACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATYGSGKTVDTTKPITVVTQ CCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCFVTDDGTSTGTLSEIRRYATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCYVQNGVVIPQPSSKISGVGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAASGNVINSDFCDAEISTFGECACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGT TASFSKHGGLAKMGAGCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCT MEAGMVLVMSLWDDYSACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACC VNMLWLDSTYPTNATGTACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAC PGAARGSCPTTSGDPKTVCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGESQSGSSYVTFSDIRVGPFCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCT NSTFSGGSSTGGSSTTTACTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGSGTTTTKASSTSTSSTSTGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACC TGVAAHWGQCGGQGWTACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA GPTTCASGTTCTVVNPY YSQCL132330 D8 GSSM Thermo-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS toleranceTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCA LLATAGAQQIGTYTAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNS 71, 72CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA GAITLDANWRWVHGVNGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TSTNCYTGNTWNTAICDGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTAC TDASCAQDCALDGADYSGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTYGITTSGNSLRLNFVT GTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGAGSNVGSRTYLMADNTHY CTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGQIFDLLNQEFTFTVDVSH TTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCALPCGLNGALYFVTMDAD AGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTGGVSKYPNNKAGAQYG CAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGVGYCDSQCPRDLKFIAGQ GACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTANVEGWTPSSNNANTGL GCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTGNHGACCAELDIWEANSICACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTSEALTPHPCDTPGLSVCTGTTTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTC TDACGGVYSSDRYAGTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGAC DPDGCDFNPYRLGVTDFACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATC YGSGKTVDTTKPITVVTQCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCA FVTDDGTSTGTLSEIRRYTCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCC YVQNGVVIPQPSSKISGVGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAASGNVINSDFCDAEISTFGECACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGT TASFSKHGGLAKMGAGCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCT MEAGMVLVMSLWDDYSACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACC VNMLWLDSTYPTNATGTACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAC PGAARGSCPTTSGDPKTVCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGESQSGSSYVTFSDIRVGPFCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCT NSTFSGGSSTGGSSTTTACTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGSGTTTTKASSTSTSSTSTGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACC TGVAAHWGQCGGQGWTACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA GPTTCASGTTCTVVNPY YSQCL131194 E5 GSSM Thermo-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS toleranceTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAGCTCA LLATAGAQQIGTYTAEASEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCHPSLSWSTCKSGGSCTTN 73, 74CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA SGAITLDANWRWVHGVGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT NTSTNCYTGNTWNTAICGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTAC DTDASCAQDCALDGADYGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACSGTYGITTSGNSLRLNFV GTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGATGSNVGSRTYLMADNTH CTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGYQIFDLLNQEFTFTVDVS TTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAHLPCGLNGALYFVTMDA AGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTDGGVSKYPNNKAGAQY CAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGVGYCDSQCPRDLKFIAG GACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTQANVEGWTPSSNNANTG GCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTLGNHGACCAELDIWEAN CACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTSISEALTPHPCDTPGLSVCACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTT TTDACGGTYSSDRYAGTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGA CDPDGCDFNPYRLGVTDCACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACAT FYGSGKTVDTTKPITVVTCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTC QFVTDDGTSTGTLSEIRRATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCYYVQNGVVIPQPSSKISGGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAAVSGNVINSDFCDAEISTFGCACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGT ETASFSKHGGLAKMGAGCATGAGTTTGTGGGACGACTACTCCGCCAACATGCTCTGGCTCGACAGCACCT MEAGMVLVMSLWDDYSACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACC ANMLWLDSTYPTNATGTACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAC PGAARGSCPTTSGDPKTVCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGESQSGSSYVTFSDIRVGPFCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCT NSTFSGGSSTGGSSTTTACTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGSGTTTTKASSTSTSSTSTGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACC TGVAAHWGQCGGQGWTACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA GPTTCASGTTCTVVNPY YSQCL132839 A3 GSSM Thermo-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS toleranceTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCA LLATAGAQQIGTYTAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNS 75, 76CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA GAITLDANWRWVHGVNGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TSTNCYTGNTWNTAICDGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTAC TDASCAQDCALDGADYSGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTYGITTSGNSLRLNFVT GTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGAGSNVGSRTYLMADNTHY CTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGQIFDLLNQEFTFTVDVSH TTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCALPCGLNGALYFVTMDAD AGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTGGVSKYPNNKAGAQYG CAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGVGYCDSQCPRDLKFIAGQ GACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTANVEGWTPSSNNANTGL GCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTGNHGACCAELDIWEANSICACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTSEALTPHPCDTPGLSVCT ACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTTDACGGTYSSDRYAGTC CAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGADPDGCDFNPYRLGVTDF CACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATYGSGKTVDTTKPITVVTQ CCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCFVTDDGTSTGTLSEIRRYATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCYVQNGVVIPQPSSKISGVGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAASGNVINSDFCDAEISTFGECACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGAC TASFSKHGGLAKMGAGTATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCT MEAGMVLTMSLWDDYSACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACC VNMLWLDSTYPTNATGTACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAC PGAARGSCPTTSGDPKTVCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGESQSGSSYVTFSDIRVGPFCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCT NSTFSGGSSTGGSSTTTACTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGSGTTTTKASSTSTSSTSTGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACC TGVAAHWGQCGGQGWTACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA GPTTCASGTTCTVVNPY YSQCL134379 H7 GSSM Thermo-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS toleranceTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCA LLATAGAQQIGTYTAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNS 77, 78CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA GAITLDANWRWVHGVNGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TSTNCYTGNTWNTAICDGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTAC TDASCAQDCALDGADYSGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTYGITTSGNSLRLNFVT GTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGAGSNVGSRTYLMADNTHY CTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGQIFDLLNQEFTFTVDVSH TTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCALPCGLNGALYFVTMDAD AGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTGGVSKYPNNKAGAQYG CAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGVGYCDSQCPRDLKFIAGQ GACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTANVEGWTPSSNNANTGL GCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTGNHGACCAELDIWEANSICACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTSEALTPHPCDTPGLSVCT ACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTTDACGGTYSSDRYAGTC CAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGADPDGCDFNPYRLGVTDF CACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATYGSGKTVDTTKPITVVTQ CCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCFVTDDGTSTGTLSEIRRYATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCYVQNGVVIPQPSSKISGVGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAASGNVINSDFCDAEISTFGECACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGT TASFSKHGGLAKMGAGCATGAGTTTGTGGGACGACGATTCCGTCAACATGCTCTGGCTCGACAGCACCT MEAGMVLVMSLWDDDSACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACC VNMLWLDSTYPTNATGTACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAC PGAARGSCPTTSGDPKTVCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGESQSGSSYVTFSDIRVGPFCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCT NSTFSGGSSTGGSSTTTACTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGSGTTTTKASSTSTSSTSTGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACC TGVAAHWGQCGGQGWTACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA GPTTCASGTTCTVVNPY YSQCL133964 C2 GSSM Thermo-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS toleranceTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCA LLATAGAQQIGTYTAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNS 79, 80CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA GAITLDANWRWVHGVNGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TSTNCYTGNTWNTAICDGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTAC TDASCAQDCALDGADYSGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTYGITTSGNSLRLNFVT GTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGAGSNVGSRTYLMADNTHY CTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGQIFDLLNQEFTFTVDVSH TTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCALPCGLNGALYFVTMDAD AGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTGGVSKYPNNKAGAQYG CAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGVGYCDSQCPRDLKFIAGQ GACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTANVEGWTPSSNNANTGL GCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTGNHGACCAELDIWEANSICACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTSEALTPHPCDTPGLSVCT ACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTTDACGGTYSSDRYAGTC CAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGADPDGCDFNPYRLGVTDF CACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATYGSGKTVDTTKPITVVTQ CCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCFVTDDGTSTGTLSEIRRYATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCYVQNGVVIPQPSSKISGVGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAASGNVINSDFCDAEISTFGECACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGT TASFSKHGGLAKMGAGCATGAGTTTGTGGGACGACTACTCCGATAACATGCTCTGGCTCGACAGCACCT MEAGMVLVMSLWDDYSACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACC DNMLWLDSTYPTNATGTACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAC PGAARGSCPTTSGDPKTVCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGESQSGSSYVTFSDIRVGPFCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCT NSTFSGGSSTGGSSTTTACTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGSGTTTTKASSTSTSSTSTGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACC TGVAAHWGQCGGQGWTACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA GPTTCASGTTCTVVNPY YSQCL133964 H3 GSSM Thermo-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS toleranceTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCA LLATAGAQQIGTYTAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNS 81, 82CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA GAITLDANWRWVHGVNGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TSTNCYTGNTWNTAICDGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTAC TDASCAQDCALDGADYSGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTYGITTSGNSLRLNFVT GTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGAGSNVGSRTYLMADNTHY CTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGQIFDLLNQEFTFTVDVSH TTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCALPCGLNGALYFVTMDAD AGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTGGVSKYPNNKAGAQYG CAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGVGYCDSQCPRDLKFIAGQ GACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTANVEGWTPSSNNANTGL GCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTGNHGACCAELDIWEANSICACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTSEALTPHPCDTPGLSVCT ACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTTDACGGTYSSDRYAGTC CAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGADPDGCDFNPYRLGVTDF CACCACCAAACCCATCACCGTTGTGACCCAATTCGTCACTGACGACGGCACATYGSGKTVDTTKPITVVTQ CCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCFVTDDGTSTGTLSEIRRYATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCYVQNGVVIPQPSSKISGVGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAASGNVINSDFCDAEISTFGECACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGC TASFSKHGGLAKMGAGCATGAGTTTGTGGGACGACTACTCCGCTAACATGCTCTGGCTCGACAGCACCT MEAGMVLAMSLWDDYSACCCTACAAACGCGACTGGTGCCCCCGGTGCCGCTCGTGGTTCCTGCCCTACC ANMLWLDSTYPTNATGAACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAC PGAARGSCPTTSGDPKTVCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGESQSGSSYVTFSDIRVGPFCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCT NSTFSGGSSTGGSSTTTACTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGSGTTTTKASSTSTSSTSTGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACC TGVAAHWGQCGGQGWTACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA GPTTCASGTTCTVVNPY YSQCL133550 C4 GSSM Thermo-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS toleranceTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCA LLATAGAQQIGTYTAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNS 83, 84CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA GAITLDANWRWVHGVNGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TSTNCYTGNTWNTAICDGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTAC TDASCAQDCALDGADYSGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTYGITTSGNSLRLNFVT GTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGAGSNVGSRTYLMADNTHY CTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGQIFDLLNQEFTFTVDVSH TTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCALPCGLNGALYFVTMDAD AGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTGGVSKYPNNKAGAQYG CAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGVGYCDSQCPRDLKFIAGQ GACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTANVEGWTPSSNNANTGL GCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTGNHGACCAELDIWEANSICACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTSEALTPHPCDTPGLSVCT ACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTTDACGGTYSSDRYAGTC CAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGADPDGCDFNPYRLGVTDF CACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATYGSGKTVDTTKPITVVTQ CCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCFVTDDGTSTGTLSEIRRYATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCYVQNGVVIPQPSSKISGVGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAASGNVINSDFCDAEISTFGECACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGT TASFSKHGGLAKMGAGCATGAGTTTGTGGGACGACTACTCCGTCAACATGACTTGGCTCGACAGCACCT MEAGMVLVMSLWDDYSACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACC VNMTWLDSTYPTNATGTACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAC PGAARGSCPTTSGDPKTVCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGESQSGSSYVTFSDIRVGPFCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCT NSTFSGGSSTGGSSTTTACTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGSGTTTTKASSTSTSSTSTGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACC TGVAAHWGQCGGQGWTACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA GPTTCASGTTCTVVNPY YSQCL133696 G4 GSSM Thermo-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS toleranceTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCA LLATAGAQQIGTYTAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNS 85, 86CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA GAITLDANWRWVHGVNGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TSTNCYTGNTWNTAICDGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTAC TDASCAQDCALDGADYSGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTYGITTSGNSLRLNFVT GTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGAGSNVGSRTYLMADNTHY CTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGQIFDLLNQEFTFTVDVSH TTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCALPCGLNGALYFVTMDAD AGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTGGVSKYPNNKAGAQYG CAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGVGYCDSQCPRDLKFIAGQ GACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTANVEGWTPSSNNANTGL GCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTGNHGACCAELDIWEANSICACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTSEALTPHPCDTPGLSVCT ACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTTDACGGTYSSDRYAGTC CAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGADPDGCDFNPYRLGVTDF CACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATYGSGKTVDTTKPITVVTQ CCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCFVTDDGTSTGTLSEIRRYATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCYVQNGVVIPQPSSKISGVGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAASGNVINSDFCDAEISTFGECACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGT TASFSKHGGLAKMGAGCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCT MEAGMVLVMSLWDDYSACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACC VNMLWLDSTYPTNATGTACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAC PGAARGSCPTTSGDPKTVCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTTAESQSGSSYVTFSDIRVGPFTACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCT NSTFSGGSYTGGSSTTTACTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGSGTTTTKASSTSTSSTSTGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACC TGVAAHWGQCGGQGWTACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA GPTTCASGTTCTVVNPY YSQCL133700 E5 GSSM Thermo-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS toleranceTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCA LLATAGAQQIGTYTAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNS 87, 88CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA GAITLDANWRWVHGVNGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TSTNCYTGNTWNTAICDGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTAC TDASCAQDCALDGADYSGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTYGITTSGNSLRLNFVT GTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGAGSNVGSRTYLMADNTHY CTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGQIFDLLNQEFTFTVDVSH TTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCALPCGLNGALYFVTMDAD AGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTGGVSKYPNNKAGAQYG CAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGVGYCDSQCPRDLKFIAGQ GACGCCCTCCTCCAACAACGTCAACACTGGACTTGGCAACCACGGAGCTTGCTANVEGWTPSSNNVNTGL GCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTGNHGACCAELDIWEANSICACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTSEALTPHPCDTPGLSVCT ACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTTDACGGTYSSDRYAGTC CAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGADPDGCDFNPYRLGVTDF CACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACGTYGSGKTVDTTKPITVVTQ CCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCFVTDDGTSTGTLSEIRRYATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCYVQNGVVIPQPSSKISGVGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAASGNVINSDFCDAEISTFGECACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGT TASFSKHGGLAKMGAGCATGAGTTTGTGGGACGACTACTCCGCCAACATGCTCTGGCTCGACAGCACCT MEAGMVLVMSLWDDYSACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACC ANMLWLDSTYPTNATGTACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAC PGAARGSCPTTSGDPKTVCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGESQSGSSYVTFSDIRVGPFCACCGGTGGCAGCTCCACTACTACCGCCAGCTGGACCACCACCACCAAGGCCT NSTFSGGSSTGGSSTTTACTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGSWTTTTKASSTSTSSTST GTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCGTGVAAHWGQCGGQGW ACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAATGPTTCASGTTCTVVNPY YSQCL 134441 A2 GSSM Thermo-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS toleranceTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCA LLATAGAQQIGTYTAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNS 89, 90CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA GAITLDANWRWVHGVNGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TSTNCYTGNTWNTAICDGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTAC TDASCAQDCALDGADYSGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTYGITTSGNSLRLNFVT GTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGAGSNVGSRTYLMADNTHY CTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGQIFDLLNQEFTFTVDVSH TTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCALPCGLNGALYFVTMDAD AGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTGGVSKYPNNKAGAQYG CAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGVGYCDSQCPRDLKFIAGQ GACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTANVEGWTPSSNNANTGL GCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTGNHGACCAELDIWEANSICACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTSEALTPHPCDTPGLSVCT ACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTTDACGGTYSSDRYAGTC CAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGADPDGCDFNPYRLGVTDF CACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATYGSGKTVDTTKPITVVTQ CCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCFVTDDGTSTGTLSEIRRYATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCYVQNGVVIPQPSSKISGVGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAASGNVINSDFCDAEISTFGECACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGT TASFSKHGGLAKMGAGCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCT MEAGMVLVMSLWDDYSACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACC VNMLWLDSTYPTNATGTACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAC PGAARGSCPTTSGDPKTVCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGESQSGSSYVTFSDIRVGPFCACCGGTGGCAGCTCCACTACTACCATGAGCGGCACCACCACCACCAAGGCCT NSTFSGGSSTGGSSTTTMCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGSGTTTTKASSTSTSSTSTGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACC TGVAAHWGQCGGQGWTACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA GPTTCASGTTCTVVNPY YSQCL135067 A2 GSSM Thermo-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS toleranceTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCA LLATAGAQQIGTYTAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNS 91, 92CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA GAITLDANWRWVHGVNGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TSTNCYTGNTWNTAICDGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTAC TDASCAQDCALDGADYSGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTYGITTSGNSLRLNFVT GTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGAGSNVGSRTYLMADNTHY CTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGQIFDLLNQEFTFTVDVSH TTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCALPCGLNGALYFVTMDAD AGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTGGVSKYPNNKAGAQYG CAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGVGYCDSQCPRDLKFIAGQ GACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTANVEGWTPSSNNANTGL GCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTGNHGACCAELDIWEANSICACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTSEALTPHPCDTPGLSVCT ACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTTDACGGTYSSDRYAGTC CAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGADPDGCDFNPYRLGVTDF CACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATYGSGKTVDTTKPITVVTQ CCACCGGCACCCTCTCCGAGATTAGACGTTACTACGTTCAGAACGGTGTTGTCFVTDDGTSTGTLSEIRRYATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCYVQNGVVIPQPSSKISGVGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAASGNVINSDFCDAEISTFGECACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGT TASFSKHGGLAKMGAGCATGAGTTTGTGGGACGACTACTCCGCCAACATGCTCTGGCTCGACAGCACCT MEAGMVLVMSLWDDYSACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACC ANMLWLDSTYPTNATGTACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAC PGAARGSCPTTSGDPKTVCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGESQSGSSYVTFSDIRVGPFCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCT NSTFSGGSSTGGSSTTTACTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGACTTGCTGCTCACTGGGSGTTTTKASSTSTSSTSTGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACC TGLAAHWGQCGGQGWTACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA GPTTCASGTTCTVVNPY YSQCLParent Thermo- ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS toleranceTTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCA LLATAGAQQIGTYTAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNS 93, 94CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA GAITLDANWRWVHGVNGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TSTNCYTGNTWNTAICDGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTAC TDASCAQDCALDGADYSGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGTYGITTSGNSLRLNFVT GTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGAGSNVGSRTYLMADNTHY CTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGQIFDLLNQEFTFTVDVSH TTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCALPCGLNGALYFVTMDAD AGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTGGVSKYPNNKAGAQYG CAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGVGYCDSQCPRDLKFIAGQ GACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTANVEGWTPSSNNANTGL GCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTGNHGACCAELDIWEANSICACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTSEALTPHPCDTPGLSVCT ACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTTDACGGTYSSDRYAGTC CAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGADPDGCDFNPYRLGVTDF CACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATYGSGKTVDTTKPITVVTQ CCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCFVTDDGTSTGTLSEIRRYATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCYVQNGVVIPQPSSKISGVGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAASGNVINSDFCDAEISTFGECACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGT TASFSKHGGLAKMGAGCATGAGTTTGTGGGACGACTCTCCGTCAACATGCTCTGGCTCGACAGCACCT MEAGMVLVMSLWDDYSACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACC VNMLWLDSTYPTNATGTACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAC PGAARGSCPTTSGDPKTVCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGESQSGSSYVTFSDIRVGPFCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCT NSTFSGGSSTGGSSTTTACTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGSGTTTTKASSTSTSSTSTGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACC TGVAAHWGQCGGQGWTACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA GPTTCASGTTCTVVNPY YSQCL

TABLE 4 % % % % % Residual Residual Residual Residual Residual MeltingMutation Activity Activity Activity Activity Activity TemperaturePlateName Well Type Mutant Property @ 60° C. @ 65° C. @ 70° C. @ 75° C.@ 80° C. ° C. 131175 B1 GSSM Thermotolerance- 97% 87% 46% 54% 56% 71.1SEQ ID 61, 62 132309 B7 GSSM Thermotolerance- 80% 39% 51% 53% 54% 68.7SEQ ID 63, 64 132309 H7 GSSM Thermotolerance- 83% 64% 60% 63% 59% 69.6SEQ ID 65, 66 131179 G5 GSSM Thermotolerance- 100%  87% 62% 71% 69% 71.6SEQ ID 67, 68 131180 D10 GSSM Thermotolerance- 107%  89% 72% 71% 74%71.2 SEQ ID 69, 70 132330 D8 GSSM Thermotolerance- 92% 65% 33% 44% 42%71.1 SEQ ID 71, 72 131194 E5 GSSM Thermotolerance- 100%  95% 55% 57% 68%73.8 SEQ ID 73, 74 132839 A3 GSSM Thermotolerance- 94% 70% 56% 54% 59%70.7 SEQ ID 75, 76 134379 H7 GSSM Thermotolerance- 91% 43% 52% 56% 58%68.7 SEQ ID 77, 78 133964 C2 GSSM Thermotolerance- 93% 88% 60% 62% 67%73.1 SEQ ID 79, 80 133964 H3 GSSM Thermotolerance- 96% 88% 71% 67% 71%74.9 SEQ ID 81, 82 133550 C4 GSSM Thermotolerance- 93% 77% 69% 69% 72%70.3 SEQ ID 83, 84 133696 G4 GSSM Thermotolerance- 99% 96% 41% 42% 48%74.2 SEQ ID 85, 86 133700 E5 GSSM Thermotolerance- 99% 96% 35% 43% 51%73.3 SEQ ID 87, 88 134441 A2 GSSM Thermotolerance- 96% 47% 28% 54% 52%70.7 SEQ ID 89, 90 135067 A2 GSSM Thermotolerance- 96% 92% 52% 61% 58%73.6 SEQ ID 91, 92 Parent Thermotolerance- 83% 26% 18% 31% 43% 69.5 SEQID 93, 94

TABLE 5 Plate Mutation Mutant Name Well Type Property NucleotideSequence AA Sequence 143588 B10 Entry- Activ-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Site ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTCTGCAGGCTGAAACCCA LLATAGAQQIGTLQAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNSG 95, 96CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCG AITLDANWRWVHGVNTACCCAGAACTGCTACGATGGCAACACTTGGAATACCGCCATCTGCGACACTGAT QNCYDGNTWNTAICDTDGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACASCAQDCALDGADYSGTYGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCCAGCAGGGCCCCGITTSGNSLRLNFVQQGPYTACTCCAAGAACGTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTAC SKNVGSRTYLMADNTHYCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACQIFDLLNQEFTFTVDVSHLCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGT PCGLNGALYFVTMDADGGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATA GVSKYPNNKAGAQYGVGCTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTYCDSQCPRDLKFIAGQAN TGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGVEGWTPSSNNANTGLGNH GAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTGACCAELDIWEANSISEALTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTPHPCDTPGLSVCTTDAC TGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGGGTYSSDRYAGTCDPDGCATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAADFNPYRLGVTDFYGSGKTGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGAVDTTKPITVVTQFVTDDG CGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGTSTGTLSEIRRYYVQNGVGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCAVIPQPSSKISGVSGNVINSDTCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTFCDAEISTFGETASFSKHGTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATG GLAKMGAGMEAGMVLVGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGAC MSLWDDYSVNMLWLDSTAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCYPTNATGTPGAARGSCPTCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATTSGDPKTVESQSGSSYVTFGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTSDIRVGPFNSTFSGGSSTGTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGSSTTTASGTTTTKASSTSGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCATSSTSTGTGVAAHWGQCG CTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGQGWTGPTTCASGTTCTV GAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAAVNPYYSQCL 143593 H9 Entry- Activ-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Site ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTCTGACCGCTGAAACCCALLATAGAQQIGTLTAETHP SEQ IDTCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCSLSWSTCKSGGSCTTNSG 97, 98CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTG AITLDANWRWVHGVNTWGACCAACTGCTACGATGGCAACACTTGGAATACCGCCATCTGCGACACTGATG TNCYDGNTWNTAICDTDACATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGSCAQDCALDGADYSGTYGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCCAGCAGGGCCCCTITTSGNSLRLNFVQQGPYSACTCCAAGAACGTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCKNVGSRTYLMADNTHYQIAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCFDLLNQEFTFTVDVSHLPCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTG GLNGALYFVTMDADGGVGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATAC SKYPNNKAGAQYGVGYCTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTDSQCPRDLKFIAGQANVE GAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGGWTPSSNNANTGLGNHG AGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTACCAELDIWEANSISEALTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTPHPCDTPGLSVCTTDACG GCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGAGTYSSDRYAGTCDPDGCDTGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGFNPYRLGVTDFYGSGKTVACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACDTTKPITVVTQFVTDDGTSGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTLSEIRRYYVQNGVVIPTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATQPSSKISGVSGNVINSDFCCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTDAEISTFGETASFSKHGGLCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGG AKMGAGMEAGMVLVMSTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACA LWDDYSVNMLWLDSTYPGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCTNATGTPGAARGSCPTTSCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGGDPKTVESQSGSSYVTFSDTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTIRVGPFNSTFSGGSSTGGSSCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGTTTASGTTTTKASSTSTSSGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCAC TSTGTGVAAHWGQCGGQTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGG GWTGPTTCASGTTCTVVNAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA PYYSQCL 143603 H11 Entry-Activ- ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Site ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATLLATAGAQQIGTYTAETH SEQ IDCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCPSLSWSTCKSGGSCTTNSG 99, 100GGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTAC AITLDANWRWVHGVNTYCAGAACTGCTACACCGGCAACACTTGGAATACCGCCATCTGCGACACTGATGC QNCYTGNTWNTAICDTDAATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGSCAQDCALDGADYSGTYGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCCAGCAGGGCCCCTAITTSGNSLRLNFVQQGPYSCTCCAAGAACGTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCAKNVGSRTYLMADNTHYQIAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTFDLLNQEFTFTVDVSHLPCCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGG GLNGALYFVTMDADGGVCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACT SKYPNNKAGAQYGVGYCGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGDSQCPRDLKFIAGQANVE AGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGWTPSSNNANTGLGNHG GCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTACCAELDIWEANSISEALTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGPHPCDTPGLSVCTTDACG CGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTYSSDRYAGTCDPDGCDGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGAFNPYRLGVTDFYGSGKTVCCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGDTTKPITVVTQFVTDDGTSGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTTGTLSEIRRYYVQNGVVIPGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCQPSSKISGVSGNVINSDFCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCDAEISTFGETASFSKHGGLAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGT AKMGAGMEAGMVLVMSCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAG LWDDYSVNMLWLDSTYPCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTNATGTPGAARGSCPTTSTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTGDPKTVESQSGSSYVTFSDCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCIRVGPFNSTFSGGSSTGGSSTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGTTTASGTTTTKASSTSTSSCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACT TSTGTGVAAHWGQCGGQGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGA GWTGPTTCASGTTCTVVNACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA PYYSQCL 143606 E8 Entry-Activ- ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Site ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTCTGTGGGCTGAAACCCA LLATAGAQQIGTLWAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNSG 101, 102CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA AITLDANWRWVHGVNTSGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TNCYTGNTWNTAICDTDAGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACSCAQDCALDGADYSGTYGGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCCAGCAGGGCCCCITTSGNSLRLNFVQQGPYSTACTCCAAGAACGTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACKNVGSRTYLMADNTHYQICAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACFDLLNQEFTFTVDVSHLPCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGT GLNGALYFVTMDADGGVGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATA SKYPNNKAGAQYGVGYCCTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTDSQCPRDLKFIAGQANVE TGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGWTPSSNNANTGLGNHG GAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTACCAELDIWEANSISEALTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCPHPCDTPGLSVCTTDACG TGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGGTYSSDRYAGTCDPDGCDATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAFNPYRLGVTDFYGSGKTVGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGADTTKPITVVTQFVTDDGTSCGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGTGTLSEIRRYYVQNGVVIPGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCAQPSSKISGVSGNVINSDFCTCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTDAEISTFGETASFSKHGGLTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATG AKMGAGMEAGMVLVMSGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGAC LWDDYSVNMLWLDSTYPAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCTNATGTPGAARGSCPTTSCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGDPKTVESQSGSSYVTFSDGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTIRVGPFNSTFSGGSSTGGSSTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAATTTASGTTTTKASSTSTSSGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCA TSTGTGVAAHWGQCGGQCTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTG GWTGPTTCASGTTCTVVNGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA PYYSQCL 143678 H8 Entry-Activ- ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Site ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTACCAGGCTGAAACCCA LLATAGAQQIGTYQAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNSG 103, 104CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCA AITLDANWRWVHGVNTSGCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGAT TNCYTGNTWNTAICDTDAGCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACSCAQDCALDGADYSGTYGGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCACCAAGGGCTCCITTSGNSLRLNFVTKGSFSSTTCTCCTCCAACATCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACNIGSRTYLMADNTHYQIFCAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACDLLNQEFTFTVDVSHLPCCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGT GLNGALYFVTMDADGGVGGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATA SKYPNNKAGAQYGVGYCCTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTDSQCPRDLKFIAGQANVE TGAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGWTPSSNNANTGLGNHG GAGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTACCAELDIWEANSISEALTTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCPHPCDTPGLSVCTTDACG TGCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGGTYSSDRYAGTCDPDGCDATGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAFNPYRLGVTDFYGSGKTVGACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGADTTKPITVVTQFVTDDGTSCGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGTGTLSEIRRYYVQNGVVIPGTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCAQPSSKISGVSGNVINSDFCTCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTDAEISTFGETASFSKHGGLTCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATG AKMGAGMEAGMVLVMSGTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGAC LWDDYSVNMLWLDSTYPAGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCTNATGTPGAARGSCPTTSCCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGDPKTVESQSGSSYVTFSDGTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTIRVGPFNSTFSGGSSTGGSSTCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAATTTASGTTTTKASSTSTSSGGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCA TSTGTGVAAHWGQCGGQCTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTG GWTGPTTCASGTTCTVVNGAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA PYYSQCL 143581 H2 Entry-Activ- ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Site ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTCAGCAGGCTGAAACCCA LLATAGAQQIGTQQAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNSG 105, 106CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTA AITLDANWRWVHGVNTYCACCAACTGCTACGATGGCAACACTTGGAATACCGCCATCTGCGACACTGATG TNCYDGNTWNTAICDTDACATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGSCAQDCALDGADYSGTYGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCACCCAGTCCGCCCITTSGNSLRLNFVTQSAQKAGAAGAACGTCGGCGCCCGTACCTACCTGATGGCCGATAACACCCACTACCAA NVGARTYLMADNTHYQIFATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCDLLNQEFTFTVDVSHLPCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGC GLNGALYFVTMDADGGVGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTG SKYPNNKAGAQYGVGYCTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGADSQCPRDLKFIAGQANVE GGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGGWTPSSNNANTGLGNHG CTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACCAELDIWEANSISEALTACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCPHPCDTPGLSVCTTDACGGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGTYSSDRYAGTCDPDGCDGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCFNPYRLGVTDFYGSGKTVGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCDTTKPITVVTQFVTDDGTSACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTTGTLSEIRRYYVQNGVVIPGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACQPSSKISGVSGNVINSDFCTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCDAEISTFGETASFSKHGGLAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTT AKMGAGMEAGMVLVMSGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCA LWDDYSVNMLWLDSTYPCCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTATNATGTPGAARGSCPTTSCCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCAGDPKTVESQSGSSYVTFSDCCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAIRVGPFNSTFSGGSSTGGSSGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTTTASGTTTTKASSTSTSSTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGG TSTGTGVAAHWGQCGGQGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAAC GWTGPTTCASGTTCTVVNCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA PYYSQCL 143458 H9 Entry-Activ- ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Site ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTGCCTACGCTGAAACCCA LLATAGAQQIGTAYAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNSG 107, 108CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTA AITLDANWRWVHGVNTYCTACAACTGCTACGATGGCAACACTTGGAATACCGCCATCTGCGACACTGATG YNCYDGNTWNTAICDTDCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGASCAQDCALDGADYSGTYGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCACCGGCTCCAACGGITTSGNSLRLNFVTGSNVTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTGSRTYLMADNTHYQIFDLTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTLNQEFTFTVDVSHLPCGL TGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGNGALYFVTMDADGGVSK TACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAYPNNKAGAQYGVGYCDS ATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGAQCPRDLKFIAGQANVEGW CGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCTPSSNNANTGLGNHGACC GCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCAAELDIWEANSISEALTPHPCCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCDTPGLSVCTTDACGGTYCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAASSDRYAGTCDPDGCDFNPCCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACYRLGVTDFYGSGKTVDTTCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACKPITVVTQFVTDDGTSTGTCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCLSEIRRYYVQNGVVIPQPSCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTSKISGVSGNVINSDFCDAEICTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGSTFGETASFSKHGGLAKM TGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGAGMEAGMVLVMSLWD GTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTADYSVNMLWLDSTYPTNA CAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGTGTPGAARGSCPTTSGDPGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGKTVESQSGSSYVTFSDIRVACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGPFNSTFSGGSSTGGSSTTGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTTASGTTTTKASSTSTSSTSCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTG TGTGVAAHWGQCGGQGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACC WTGPTTCASGTTCTVVNPGTCGTGAACCCTTACTACTCTCAATGTTTGTAA YYSQCL 143496 H1 Entry- Activ-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Site ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTCAGCAGGCTGAAACCCA LLATAGAQQIGTQQAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNSG 109, 110CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTA AITLDANWRWVHGVNTYCTACAACTGCTACGATGGCAACACTTGGAATACCGCCATCTGCGACACTGATG YNCYDGNTWNTAICDTDCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGASCAQDCALDGADYSGTYGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCACCGGCTCCAACGGITTSGNSLRLNFVTGSNVTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTGSRTYLMADNTHYQIFDLTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTLNQEFTFTVDVSHLPCGL TGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGNGALYFVTMDADGGVSK TACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAYPNNKAGAQYGVGYCDS ATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGAQCPRDLKFIAGQANVEGW CGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCTPSSNNANTGLGNHGACC GCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCAAELDIWEANSISEALTPHPCCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCDTPGLSVCTTDACGGTYCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAASSDRYAGTCDPDGCDFNPCCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACYRLGVTDFYGSGKTVDTTCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACKPITVVTQFVTDDGTSTGTCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCLSEIRRYYVQNGVVIPQPSCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTSKISGVSGNVINSDFCDAEICTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGSTFGETASFSKHGGLAKM TGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGAGMEAGMVLVMSLWD GTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTADYSVNMLWLDSTYPTNA CAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGTGTPGAARGSCPTTSGDPGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGKTVESQSGSSYVTFSDIRVACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGPFNSTFSGGSSTGGSSTTGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTTASGTTTTKASSTSTSSTSCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTG TGTGVAAHWGQCGGQGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACC WTGPTTCASGTTCTVVNPGTCGTGAACCCTTACTACTCTCAATGTTTGTAA YYSQCL 143497 A9 Entry- Activ-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Site ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTACTGGGCTGAAACCCA LLATAGAQQIGTYWAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNSG 111, 112CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTC AITLDANWRWVHGVNTSCTGGAACTGCTACGATGGCAACACTTGGAATACCGCCATCTGCGACACTGATG WNCYDGNTWNTAICDTDCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGASCAQDCALDGADYSGTYGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCACCGGCTCCAACGGITTSGNSLRLNFVTGSNVTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTGSRTYLMADNTHYQIFDLTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTLNQEFTFTVDVSHLPCGL TGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGNGALYFVTMDADGGVSK TACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAYPNNKAGAQYGVGYCDS ATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGAQCPRDLKFIAGQANVEGW CGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCTPSSNNANTGLGNHGACC GCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCAAELDIWEANSISEALTPHPCCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCDTPGLSVCTTDACGGTYCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAASSDRYAGTCDPDGCDFNPCCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACYRLGVTDFYGSGKTVDTTCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACKPITVVTQFVTDDGTSTGTCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCLSEIRRYYVQNGVVIPQPSCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTSKISGVSGNVINSDFCDAEICTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGSTFGETASFSKHGGLAKM TGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGAGMEAGMVLVMSLWD GTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTADYSVNMLWLDSTYPTNA CAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGTGTPGAARGSCPTTSGDPGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGKTVESQSGSSYVTFSDIRVACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGPFNSTFSGGSSTGGSSTTGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTTASGTTTTKASSTSTSSTSCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTG TGTGVAAHWGQCGGQGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACC WTGPTTCASGTTCTVVNPGTCGTGAACCCTTACTACTCTCAATGTTTGTAA YYSQCL 143461 H2 Entry- Activ-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Site ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTGCCCAGGCTGAAACCCA LLATAGAQQIGTAQAETHSEQ ID TCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCPSLSWSTCKSGGSCTTNSG 113, 114CGGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTC AITLDANWRWVHGVNTSCTACAACTGCTACGATGGCAACACTTGGAATACCGCCATCTGCGACACTGATG YNCYDGNTWNTAICDTDCATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGASCAQDCALDGADYSGTYGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCACCGGCTCCAACGGITTSGNSLRLNFVTGSNVTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTGSRTYLMADNTHYQIFDLTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTLNQEFTFTVDVSHLPCGL TGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGNGALYFVTMDADGGVSK TACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAYPNNKAGAQYGVGYCDS ATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGAQCPRDLKFIAGQANVEGW CGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCTPSSNNANTGLGNHGACC GCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCAAELDIWEANSISEALTPHPCCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCDTPGLSVCTTDACGGTYCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAASSDRYAGTCDPDGCDFNPCCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACYRLGVTDFYGSGKTVDTTCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACKPITVVTQFVTDDGTSTGTCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCLSEIRRYYVQNGVVIPQPSCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTSKISGVSGNVINSDFCDAEICTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGSTFGETASFSKHGGLAKM TGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGAGMEAGMVLVMSLWD GTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTADYSVNMLWLDSTYPTNA CAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGTGTPGAARGSCPTTSGDPGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGKTVESQSGSSYVTFSDIRVACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGPFNSTFSGGSSTGGSSTTGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTTASGTTTTKASSTSTSSTSCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTG TGTGVAAHWGQCGGQGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACC WTGPTTCASGTTCTVVNPGTCGTGAACCCTTACTACTCTCAATGTTTGTAA YYSQCL 143602 H11 Entry- Activ-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Site ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATLLATAGAQQIGTYTAETH SEQ IDCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCPSLSWSTCKSGGSCTTNSG 115, 116GGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTG AITLDANWRWVHGVNTWGCAGAACTGCTACACCGGCAACACTTGGAATACCGCCATCTGCGACACTGATG QNCYTGNTWNTAICDTDACATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGSCAQDCALDGADYSGTYGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCCAGCAGGGCCCCTITTSGNSLRLNFVQQGPYSACTCCAAGAACGTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCKNVGSRTYLMADNTHYQIAAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCFDLLNQEFTFTVDVSHLPCTCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTG GLNGALYFVTMDADGGVGCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATAC SKYPNNKAGAQYGVGYCTGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTDSQCPRDLKFIAGQANVE GAGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGGWTPSSNNANTGLGNHG AGCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTACCAELDIWEANSISEALTTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTPHPCDTPGLSVCTTDACG GCGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGAGTYSSDRYAGTCDPDGCDTGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGFNPYRLGVTDFYGSGKTVACCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACDTTKPITVVTQFVTDDGTSGGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTLSEIRRYYVQNGVVIPTGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATQPSSKISGVSGNVINSDFCCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTDAEISTFGETASFSKHGGLCAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGG AKMGAGMEAGMVLVMSTCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACA LWDDYSVNMLWLDSTYPGCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCTNATGTPGAARGSCPTTSCTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGGDPKTVESQSGSSYVTFSDTCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTIRVGPFNSTFSGGSSTGGSSCTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGTTTASGTTTTKASSTSTSSGCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCAC TSTGTGVAAHWGQCGGQTGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGG GWTGPTTCASGTTCTVVNAACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA PYYSQCL 143606 A11 Entry-Activ- ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Site ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTCTGTACGCTGAAACCCATLLATAGAQQIGTLYAETH SEQ IDCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCPSLSWSTCKSGGSCTTNSG 117, 118GGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCTCC AITLDANWRWVHGVNTSACCAACTGCTACGATGGCAACACTTGGAATACCGCCATCTGCGACACTGATGC TNCYDGNTWNTAICDTDAATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGGSCAQDCALDGADYSGTYGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTCCAGCAGGGCCCCTAITTSGNSLRLNFVQQGPYSCTCCAAGAACGTCGGCTCCCGTACCTACCTGATGGCCGATAACACCCACTACCAKNVGSRTYLMADNTHYQIAATCTTCGACTTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTFDLLNQEFTFTVDVSHLPCCCCTTGCGGTTTGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGG GLNGALYFVTMDADGGVCGTCTCCAAGTACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACT SKYPNNKAGAQYGVGYCGTGACTCTCAATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGDSQCPRDLKFIAGQANVE AGGGCTGGACGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGWTPSSNNANTGLGNHG GCTTGCTGCGCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTACCAELDIWEANSISEALTGACTCCTCACCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGPHPCDTPGLSVCTTDACG CGGTGGTACCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTYSSDRYAGTCDPDGCDGTGACTTCAACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGAFNPYRLGVTDFYGSGKTVCCGTTGACACCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGDTTKPITVVTQFVTDDGTSGCACATCCACCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTTGTLSEIRRYYVQNGVVIPGTTGTCATCCCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCQPSSKISGVSGNVINSDFCAACTCCGACTTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCDAEISTFGETASFSKHGGLAGCAAACACGGTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGT AKMGAGMEAGMVLVMSCTTGGTCATGAGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAG LWDDYSVNMLWLDSTYPCACCTACCCTACAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTNATGTPGAARGSCPTTSTACCACTTCTGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTGDPKTVESQSGSSYVTFSDCACCTTTTCTGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCIRVGPFNSTFSGGSSTGGSSTAGCACCGGTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGTTTASGTTTTKASSTSTSSCCTCTTCCACCTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACT TSTGTGVAAHWGQCGGQGGGGTCAGTGTGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGA GWTGPTTCASGTTCTVVNACCACATGCACCGTCGTGAACCCTTACTACTCTCAATGTTTGTAA PYYSQCL 156605 H4 ParentActiv- ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATLLATAGAQQIGTYTAETH SEQ IDCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCPSLSWSTCKSGGSCTTNSG 119, 120GGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAG AITLDANWRWVHGVNTSCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATG TNCYTGNTWNTAICDTDACATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGSCAQDCALDGADYSGTYGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGITTSGNSLRLNFVTGSNVGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTSRTYLMADNTHYQIFDLLTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTNQEFTFTVDVSHLPCGLN TGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGGALYFVTMDADGGVSKY TACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAPNNKAGAQYGVGYCDSQ ATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACPRDLKFIAGQANVEGWT CGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCPSSNNANTGLGNHGACCA GCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCAELDIWEANSISEALTPHPCCCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACDTPGLSVCTTDACGGTYSCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAASDRYAGTCDPDGCDFNPYCCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACRLGVTDFYGSGKTVDTTKCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACPITVVTQFVTDDGTSTGTLCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCSEIRRYYVQNGVVIPQPSSCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTKISGVSGNVINSDFCDAEISCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTFGETASFSKHGGLAKMG TGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAAGMEAGMVLVMSLWDD GTTTGTGGGATGATTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTAYSVNMLWLDSTYPTNAT CAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGTPGAARGSCPTTSGDPKGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGTVESQSGSSYVTFSDIRVGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGPFNSTFSGGSSTGGSSTTTGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTASGTTTTKASSTSTSSTSTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTG GTGVAAHWGQCGGQGWGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACC TGPTTCASGTTCTVVNPYGTCGTGAACCCTTACTACTCTCAATGTTTGTAA YSQCL 159293 E7 Point Activ-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Mutant ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATLLATAGAQQIGTYTAETH Recombi- SEQ IDCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCPSLSWSTCKSGGSCTTNSG nation 121, 122GGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAG AITLDANWRWVHGVNTSCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATG TNCYTGNTWNTAICDTDACATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGSCAQDCALDGADYSGTYGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGITTSGNSLRLNFVTGSNVGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTSRTYLMADNTHYQIFDLLTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCGGGTGCGGTTNQEFTFTVDVSHLGCGLN TGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGGALYFVTMDADGGVSKY TACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAPNNKAGAQYGVGYCDSQ ATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACPRDLKFIAGQANVEGWT CGCCCAAGTCCAACAACGCCCATACTGGATATGGCAACCACGGAGCTTGCTGCPKSNNAHTGYGNHGACC GCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCAAELDIWEANSISEALTPHPCCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCDTPGLSVCTTDACGGTYCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAASSDRYAGTCDPDGCDFNPCCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACYRLGVTDFYGSGKTVDTTCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACKPITVVTQFVTDDGTSTGTCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCLSEIRRYYVQNGVVIPQPSCCAGCCTTCCTCCGATATCTCCGGAGTCAGCGGAGTTGTCATCAACTCCGACTTSDISGVSGVVINSDFCDAEICTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGSTFGETASFSKHGGLAKM TGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGAGMEAGMVLVMSLWD GTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTADYSVNMLWLDSTYPTNA CAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGTGTPGAARGSCPTTSGDPGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGKTVESQSGSSYVTFSDIRWACATCCGGTGGGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGPFNSTFSGGSSTGGSSTTGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTTASGTTTTKASSTSTSSTSCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTG TGTGVAAHWGQCGGQGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACC WTGPTTCASGTTCTVVNPGTCGTGAACCCTTACTACTCTCAATGTTTGTAA YYSQCL 159294 E3 Point Activ-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Mutant ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATLLATAGAQQIGTYTAETH Recombi- SEQ IDCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCPSLSWSTCKSGGSCTTNSG nation 123, 124GGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAG AITLDANWRWVHGVNTSCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATG TNCYTGNTWNTAICDTDACATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGSCAQDCALDGADYSGTYGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGITTSGNSLRLNFVTGSNVGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTSRTYLMADNTHYQIFDLLTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTNQEFTFTVDVSHLPCGLN TGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGGALYFVTMDADGGVSKY TACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAPNNKAGAQYGVGYCDSQ ATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACPRDLKFIAGQANVEGWT CGCCCTCCTCCAACAACGCCCATACTGGATATGGCAACCACGGAGCTTGCTGCPSSNNAHTGYGNHGACCA GCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCAELDIWEANSISEALTPHPCCCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACDTPGLSVCTTDACGGTYSCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAASDRYAGTCDPDGCDFNPYCCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACRLGVTDFYGSGKTVDTTKCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACPITVVTQFVTDDGTSTGTLCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCSEIRRYYVQNGVVIPQPSSCCAGCCTTCCTCCGATATCTCCGGAGTCAGCGGAGTTGTCATCAACTCCGACTTDISGVSGVVINSDFCDAEISCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTFGETASFSKHGGLAKMG TGGCCTGGCAAAGATGGGCGCTGGTATGAGTGCTGGTATGGTCTTGGTCATGAAGMSAGMVLVMSLWDD GTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTAYSVNMLWLDSTYPTNAT CAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGTPGAARGSCPTTSGDPKGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGTVESQSGSSYVTFSDIRWGACATCCGGTGGGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGPFNSTFSGGSSTGGSSTTTGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTASGTTTTKASSTSTSSTSTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTG GTGVAAHWGQCGGQGWGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACC TGPTTCASGTTCTVVNPYGTCGTGAACCCTTACTACTCTCAATGTTTGTAA YSQCL 159294 G10 Point Activ-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Mutant ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATLLATAGAQQIGTYTAETH Recombi- SEQ IDCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCPSLSWSTCKSGGSCTTNSG nation 125, 126GGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAG AITLDANWRWVHGVNTSCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATG TNCYTGNTWNTAICDTDACATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGSCAQDCALDGADYSGTYGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGITTSGNSLRLNFVTGSNVGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTSRTYLMADNTHYQIFDLLTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTNQEFTFTVDVSHLPCGLN TGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGGALYFVTMDADGGVSKY TACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAPNNKAGAQYGVGYCDSQ ATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACPRDLKFIAGQANVEGWT CGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCPSSNNANTGLGNHGACCA GCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCAELDIWEANSISEALTPHPCCCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACDTPGLSVCTTDACGGTYSCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAASDRYAGTCDPDGCDFNPYCCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACRLGVTDFYGSGKTVDTTKCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACPITVVTQFVTDDGTSTGTLCGGCACCCTCCTTGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCLEIRRYYVQNGVVIPQPSSCCAGCCTTCCTCCGATATCTCCGGAGTCAGCGGAGTTGTCATCAACTCCGACTTDISGVSGVVINSDFCDAEISCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTFGETASFSKHGGLAKMG TGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAAGMEAGMVLVMSLWDD GTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTAYSVNMLWLDSTYPTNAT CAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGTPGAARGSCPTTSGDPKGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGTVESQSGSSYVTFSDIRVGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGPFNSTFSGGSSTGGSSTTTGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTASGTTTTKASSTSTSSTSTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTG GTGVAAHWGQCGGQGWGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACC TGPTTCASGTTCTVVNPYGTCGTGAACCCTTACTACTCTCAATGTTTGTAA YSQCL 159297 B8 Point Activ-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Mutant ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATLLATAGAQQIGTYTAETH Recombi- SEQ IDCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCPSLSWSTCKSGGSCTTNSG nation 127, 128GGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAG AITLDANWRWVHGVNTSCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATG TNCYTGNTWNTAICDTDACATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGSCAQDCALDGADYSGTYGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGITTSGNSLRLNFVTGSNVGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTSRTYLMADNTHYQIFDLLTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTNQEFTFTVDVSHLPCGLN TGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGGALYFVTMDADGGVSKY TACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAPNNKAGAQYGVGYCDSQ ATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACPRDLKFIAGQANVEGWT CGCCCTCCTCCAACAACGCCAACACTGGATATGGCAACCACGGAGCTTGCTGCPSSNNANTGYGNHGACCA GCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCAELDIWEANSISEALTPHPCCCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACDTPGLSVCTTDACGGTYSCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAASDRYAGTCDPDGCDFNPYCCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACRLGVTDFYGSGKTVDTTKCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACCAGGGCACATCCACPITVVTQFVTDQGTSTGRLCGGCCGTCTCCTTGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCLEIRRYYVQNGVVIPQPSSCCAGCCTTCCTCCGATATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTDISGVSGNVINSDFCDAEISCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTFGETASFSKHGGLAKMG TGGCCTGGCAAAGATGGGCGCTGGTATGAGTGCTGGTATGGTCTTGGTCATGAAGMSAGMVLVMSLWDD GTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTAYSVNMLWLDSTYPTNAT CAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGTPGAARGSCPTTSGDPKGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGTVESQSGSSYVTFSDIRVGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGPFNSTFSGGSSTGGSSTTTGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTASGTTTTKASSTSTSSTSTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTG GTGVAAHWGQCGGQGWGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACC TGPTTCASGTTCTVVNPYGTCGTGAACCCTTACTACTCTCAATGTTTGTAA YSQCL 159305 E7 Point Activ-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Mutant ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATLLATAGAQQIGTYTAETH Recombi- SEQ IDCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCPSLSWSTCKSGGSCTTNSG nation 129, 130GGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAG AITLDANWRWVHGVNTSCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATG TNCYTGNTWNTAICDTDACATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGSCAQDCALDGADYSGTYGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGITTSGNSLRLNFVTGSNVGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTSRTYLMADNTHYQIFDLLTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCGGGTGCGGTTNQEFTFTVDVSHLGCGLN TGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGGALYFVTMDADGGVSKY TACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAPNNKAGAQYGVGYCDSQ ATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACPRDLKFIAGQANVEGWT CGCCCAAGTCCAACAACGCCCATACTGGATATGGCAACCACGGAGCTTGCTGCPKSNNAHTGYGNHGACC GCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCAAELDIWEANSISEALTPHPCCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACCDTPGLSVCTTDACGGTYCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAASSDRYAGTCDPDGCDFNPCCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACYRLGVTDFYGSGKTVDTTCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACKPITVVTQFVTDDGTSTGTCGGCACCCTCTCCGAGATCAGACGTTACTACGTTAGTAACGGTGTTGTCATCCCLSEIRRYYVSNGVVIPQPSCCAGCCTTCCTCCGATATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTSDISGVSGNVINSDFCDAEICTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGSTFGETASFSKHGGLAKM TGGCCTGGCAAAGATGGGCGCTGGTATGAGTGCTGGTATGGTCTTGGTCATGAGAGMSAGMVLVMSLWD GTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTADYSVNMLWLDSTYPTNA CAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGTGTPGAARGSCPTTSGDPGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGKTVESQSGSSYVTFSDIRVACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGGPFNSTFSGGSSTGGSSTTGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTTASGTTTTKASSTSTSSTSCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTG TGTGVAAHWGQCGGQGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACC WTGPTTCASGTTCTVVNPGTCGTGAACCCTTACTACTCTCAATGTTTGTAA YYSQCL 159734 B5 Point Activ-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Mutant ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATLLATAGAQQIGTYTAETH Recombi- SEQ IDCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCPSLSWSTCKSGGSCTTNSG nation 131, 132GGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAG AITLDANWRWVHGVNTSCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATG TNCYTGNTWNTAICDTDACATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGSCAQDCALDGADYSGTYGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGITTSGNSLRLNFVTGSNVGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTSRTYLMADNTHYQIFDLLTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTNQEFTFTVDVSHLPCGLN TGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGGALYFVTMDADGGVSKY TACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAPNNKAGAQYGVGYCDSQ ATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACPRDLKFIAGQANVEGWT CGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCPSSNNANTGLGNHGACCA GCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCAELDIWEANSISEALTPHPCCCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACDTPGLSVCTTDACGGTYSCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAASDRYAGTCDPDGCDFNPYCCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACRLGVTDFYGSGKTVDTTKCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACPITVVTQFVTDDGTSTGTLCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCSEIRRYYVQNGVVIPQPSSCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTKISGVSGNVINSDFCDAEISCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTFGETASFSKHGGLAKMG TGGCCTGGCAAAGATGGGCGCTGGTATGAGTGCTGGTATGGTCTTGGTCATGAAGMSAGMVLVMSLWDD GTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTAYSVNMLWLDSTYPTNAT CAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGTPGAARGSCPTTSGDPKGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGTVESQSGSSYVTFSDIRWGACATCCGGTGGGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGPFNSTFSGGSSTGGSSTTTGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTASGTTTTKASSTSTSSTSTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTG GTGVAAHWGQCGGQGWGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACC TGPTTCASGTTCTVVNPYGTCGTGAACCCTTACTACTCTCAATGTTTGTAA YSQCL Product Activ-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS Release ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATLLATAGAQQIGTYTAETH Site SEQ IDCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCPSLSWSTCKSGGSCTTNSG 135, 136GGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAG AITLDANWRWVHGVNTSCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATG TNCYTGNTWNTAICDTDACATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGSCAQDCALDGADYSGTYGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGITTSGNSLRLNFVTGSNVGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTSRTYLMADNTHYQIFDLLTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTNQEFTFTVDVSHLPCGLN TGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGGALYFVTMDADGGVSKY TACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAPNNKAGAQYGVGYCDSQ ATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACPRDLKFIAGQANVEGWT CGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCPSSNNANTGLGNHGACCA GCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCAELDIWEANSISEALTPHPCCCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACDTPGLSVCTTDACGGTYS CTACAGCTCCGATAAGTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCASDKYAGTCDPDGCDFNPYACCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACARLGVTDFYGSGKTVDTTKCCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCAPITVVTQFVTDDGTSTGTLCCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCSEIRRYYVQNGVVIPQPSSCCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTKISGVSGNVINSDFCDAEISTCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGTFGETASFSKHGGLAKMG GTGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAGMEAGMVLVMSLWDD AGTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTYSVNMLWLDSTYPTNAT ACAAACGCGACTGGTACCCCCGGTGCCGCTAAGGGTTCCTGCCCTACCACTTCTGTPGAAKGSCPTTSGDPKGGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTTVESQSGSSYVTFSDIRVGGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTPFNSTFSGGSSTGGSSTTTGGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCASGTTTTKASSTSTSSTSTTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGT GTGVAAHWGQCGGQGWGGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCAC TGPTTCASGTTCTVVNPYCGTCGTGAACCCTTACTACTCTCAATGTTTGTAG YSQCL Parent Activ-ATGTCTGCCTTGAACTCTTTCAATATGTACAAGAGCGCCCTCATCTTGGGCTCCMSALNSFNMYKSALILGS ity-TTGCTGGCAACAGCTGGTGCTCAGCAAATTGGTACTTATACCGCTGAAACCCATLLATAGAQQIGTYTAETH SEQ IDCCCTCTTTGAGCTGGTCTACTTGCAAATCGGGTGGTAGCTGCACCACAAACTCCPSLSWSTCKSGGSCTTNSG 133, 134GGTGCCATTACGTTGGATGCCAACTGGCGTTGGGTCCATGGTGTCAATACCAG AITLDANWRWVHGVNTSCACCAACTGCTACACTGGCAACACTTGGAATACCGCCATCTGCGACACTGATG TNCYTGNTWNTAICDTDACATCCTGTGCCCAGGACTGTGCTCTTGATGGTGCTGACTACTCTGGCACGTACGSCAQDCALDGADYSGTYGGTATCACTACCTCCGGCAACTCATTGCGCCTGAACTTCGTTACCGGTTCCAACGITTSGNSLRLNFVTGSNVGTCGGATCTCGTACCTACCTGATGGCCGATAACACCCACTACCAAATCTTCGACTSRTYLMADNTHYQIFDLLTGTTGAACCAGGAGTTCACTTTCACCGTCGATGTCTCCCACCTCCCTTGCGGTTNQEFTFTVDVSHLPCGLN TGAACGGTGCCCTCTACTTCGTGACCATGGACGCCGACGGTGGCGTCTCCAAGGALYFVTMDADGGVSKY TACCCCAACAACAAGGCCGGCGCTCAGTACGGTGTTGGATACTGTGACTCTCAPNNKAGAQYGVGYCDSQ ATGCCCTCGTGACTTGAAATTCATCGCTGGTCAGGCCAACGTTGAGGGCTGGACPRDLKFIAGQANVEGWT CGCCCTCCTCCAACAACGCCAACACTGGACTTGGCAACCACGGAGCTTGCTGCPSSNNANTGLGNHGACCA GCAGAGCTTGATATCTGGGAGGCAAACAGCATCTCAGAGGCTTTGACTCCTCAELDIWEANSISEALTPHPCCCCTTGCGATACACCCGGTCTATCTGTTTGCACTACTGATGCCTGCGGTGGTACDTPGLSVCTTDACGGTYSCTACAGCTCCGATCGTTACGCCGGTACCTGCGACCCTGATGGATGTGACTTCAASDRYAGTCDPDGCDFNPYCCCTTACCGTCTTGGTGTCACTGACTTCTACGGCTCCGGCAAGACCGTTGACACRLGVTDFYGSGKTVDTTKCACCAAACCCATCACCGTTGTGACTCAATTCGTCACTGACGACGGCACATCCACPITVVTQFVTDDGTSTGTLCGGCACCCTCTCCGAGATCAGACGTTACTACGTTCAGAACGGTGTTGTCATCCCSEIRRYYVQNGVVIPQPSSCCAGCCTTCCTCCAAGATCTCCGGAGTCAGCGGAAATGTCATCAACTCCGACTTKISGVSGNVINSDFCDAEISCTGCGATGCTGAGATCTCCACCTTTGGCGAGACTGCCTCCTTCAGCAAACACGGTFGETASFSKHGGLAKMG TGGCCTGGCAAAGATGGGCGCTGGTATGGAAGCTGGTATGGTCTTGGTCATGAAGMEAGMVLVMSLWDD GTTTGTGGGACGACTACTCCGTCAACATGCTCTGGCTCGACAGCACCTACCCTAYSVNMLWLDSTYPTNAT CAAACGCGACTGGTACCCCCGGTGCCGCTCGTGGTTCCTGCCCTACCACTTCTGGTPGAARGSCPTTSGDPKGGGACCCTAAGACCGTTGAATCACAATCCGGCAGCTCCTATGTCACCTTTTCTGTVESQSGSSYVTFSDIRVGACATCCGGGTTGGTCCTTTCAACTCTACGTTCAGCGGTGGTTCTAGCACCGGTGPFNSTFSGGSSTGGSSTTTGCAGCTCCACTACTACCGCCAGCGGCACCACCACCACCAAGGCCTCTTCCACCTASGTTTTKASSTSTSSTSTCTACTTCCAGCACCTCTACCGGCACTGGAGTCGCTGCTCACTGGGGTCAGTGTG GTGVAAHWGQCGGQGWGTGGCCAGGGTTGGACTGGTCCTACCACCTGCGCTAGTGGAACCACATGCACC TGPTTCASGTTCTVVNPYGTCGTGAACCCTTACTACTCTCAATGTTTGTAA YSQCL

TABLE 6 % % improvement improvement Plate over WT @ over WT @ Dose NameWell Mutation Type Mutant Property 48 hr 72 hr Reduction 143588 B10EntrySite Activity-SEQ ID 95, 96 10.3% NA 143593 H9 EntrySiteActivity-SEQ ID 97, 98 8.5% NA 143603 H11 EntrySite Activity-SEQ ID 99,100 6.7% NA  0.5X 143606 E8 EntrySite Activity-SEQ ID 101, 102 10.9% NA143678 H8 EntrySite Activity-SEQ ID 103, 104 15.9% NA 143581 H2EntrySite Activity-SEQ ID 105, 106 11.8% NA  0.5X 143458 H9 EntrySiteActivity-SEQ ID 107, 108 23.2% NA 0.75X 143496 H1 EntrySite Activity-SEQID 109, 110 11.9% NA 143497 A9 EntrySite Activity-SEQ ID 111, 112 9.5%NA 143461 H2 EntrySite Activity-SEQ ID 113, 114 22.2% NA  0.8X 143602H11 EntrySite Activity-SEQ ID 115, 116 18.3% NA 0.75X 143606 A11EntrySite Activity-SEQ ID 117, 118 7.9% NA 156605 H4 Loop GeneReassemblyActivity-SEQ ID 119, 120 18.1% NA 159293 E7 PointMutantRecombinationActivity-SEQ ID 121, 122 NA  5.4% 159294 E3 PointMutantRecombinationActivity-SEQ ID 123, 124 NA 19.6% 0.75X 159294 G10PointMutantRecombination Activity-SEQ ID 125, 126 NA 18.6%  0.6X 159297B8 PointMutantRecombination Activity-SEQ ID 127, 128 NA 19.2%   1X159305 E7 PointMutantRecombination Activity-SEQ ID 129, 130 NA 17.2%0.65X 159734 B5 PointMutantRecombination Activity-SEQ ID 131, 132 NA12.2% 0.75X PointMutantRecombination Activity-SEQ ID 135, 136 N/A N/AN/A Parent Activity-SEQ ID 133, 134 NULL NULL NULL

The invention is further described by the embodiments of followingnumbered paragraphs. Most embodiments relate to CBH I polypeptides, CBHI nucleic acids, and their uses. The CBH I polypeptides are preferablyvariant CBH I polypeptides with improved characteristics relative toBD29555, such as improved activity, thermal tolerance or productinhibition. The polypeptides preferably include one or more of thesubstitutions (or combinations of substitutions) described in Table Aand in the Summary. The nucleic acids preferably encode such variant CBHI polypeptides, and the uses (e.g., methods of making fuel) also employthe variant CBH I polypeptides described herein.

1. An isolated, synthetic or recombinant nucleic acid comprising

(a) a nucleic acid sequence (polynucleotide) having at least 50%, 51%,52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%,66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%,80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%,94%, 95%, 96%, 97%, 98%, 99%, or more or complete (100%) sequenceidentity to SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ IDNO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:17, SEQ IDNO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ IDNO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ IDNO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ IDNO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ IDNO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ IDNO:69, SEQ ID NO:71, SEQ ID NO:73, SEQ ID NO:75, SEQ ID NO:77, SEQ IDNO:79, SEQ ID NO:81, SEQ ID NO:83, SEQ ID NO:85, SEQ ID NO:87, SEQ IDNO:89, SEQ ID NO:91, SEQ ID NO:93, SEQ ID NO:95, SEQ ID NO:97, SEQ IDNO:99, SEQ ID NO:101, SEQ ID NO:103, SEQ ID NO:105, SEQ ID NO:107, SEQID NO:109, SEQ ID NO:111, SEQ ID NO:113, SEQ ID NO:115, SEQ ID NO:117,SEQ ID NO:119, SEQ ID NO:121, SEQ ID NO:123, SEQ ID NO:125, SEQ IDNO:127, SEQ ID NO:129, SEQ ID NO:131, SEQ ID NO:133, and/or SEQ IDNO:135, over a region of at least about 20, 30, 40, 50, 75, 100, 150,200, 250, 300, 350, 400, 450, 500, 550, 600, 650, 700, 750, 800, 850,900, 950, 1000, 1050, 1100, 1150 or more residues, or the full length ofa cDNA, transcript (mRNA) or gene,

wherein optionally the nucleic acid (polynucleotide) encodes apolypeptide having a lignocellulosic activity, or encodes a polypeptideor peptide capable of generating an antibody that specifically binds toSEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ IDNO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ IDNO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ IDNO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ IDNO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ IDNO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ IDNO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ IDNO:72, SEQ ID NO:74, SEQ ID NO:76, SEQ ID NO:78, SEQ ID NO:80, SEQ IDNO:82, SEQ ID NO:84, SEQ ID NO:86, SEQ ID NO:88, SEQ ID NO:90, SEQ IDNO:92, SEQ ID NO:94, SEQ ID NO:96, SEQ ID NO:98, SEQ ID NO:100, SEQ IDNO:102, SEQ ID NO:104, SEQ ID NO:106, SEQ ID NO:108, SEQ ID NO:110, SEQID NO:112, SEQ ID NO:114, SEQ ID NO:116, SEQ ID NO:118, SEQ ID NO:120,SEQ ID NO:122, SEQ ID NO:124, SEQ ID NO:126, SEQ ID NO:128, SEQ IDNO:130, SEQ ID NO:132 and/or SEQ ID NO:134, and/or enzymatically activesubsequences (fragments) thereof,

wherein optionally the lignocellulosic activity comprises a cellulase, acellulolytic activity or a cellobiohydrolase activity,

and optionally the sequence identities are determined by analysis with asequence comparison algorithm or by a visual inspection,

and optionally the sequence comparison algorithm comprises a BLASTversion 2.2.2 algorithm where a filtering setting is set to blastall -pblastp -d “nr pataa”-F F, and all other options are set to default;

(b) a nucleic acid sequence (a polynucleotide) that hybridizes understringent conditions to the nucleic acid of (a), wherein the nucleicacid encodes a polypeptide having a lignocellulosic activity, andoptionally the lignocellulosic activity comprises a cellulase, acellulolytic activity or a cellobiohydrolase activity,

and the stringent conditions comprise a wash step comprising a wash in0.2×SSC at a temperature of about 65° C. for about 15 minutes,

and optionally the nucleic acid is at least about 20, 30, 40, 50, 60,75, 100, 150, 200, 300, 400, 500, 600, 700, 800, 900, 1000 or moreresidues in length or the full length of the gene, cDNA or transcript(mRNA);

(c) a nucleic acid sequence encoding a polypeptide having the sequenceof SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ IDNO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ IDNO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ IDNO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ IDNO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ IDNO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ IDNO:72, SEQ ID NO:74, SEQ ID NO:76, SEQ ID NO:78, SEQ ID NO:80, SEQ IDNO:82, SEQ ID NO:84, SEQ ID NO:86, SEQ ID NO:88, SEQ ID NO:90, SEQ IDNO:92, SEQ ID NO:94, SEQ ID NO:96, SEQ ID NO:98, SEQ ID NO:100, SEQ IDNO:102, SEQ ID NO:104, SEQ ID NO:106, SEQ ID NO:108, SEQ ID NO:110, SEQID NO:112, SEQ ID NO:114, SEQ ID NO:116, SEQ ID NO:118, SEQ ID NO:120,SEQ ID NO:122, SEQ ID NO:124, SEQ ID NO:126, SEQ ID NO:128, SEQ IDNO:130, SEQ ID NO:132, SEQ ID NO:134, and/or SEQ ID NO:136, orenzymatically active subsequences (fragments) thereof;

(d) the nucleic acid (polynucleotide) of (a), (b) or (c) and encoding apolypeptide having at least one conservative amino acid substitution andretaining its lignocellulosic activity,

wherein optionally the conservative amino acid substitution comprisesubstituting an amino acid with another amino acid of likecharacteristics, and optionally a conservative substitution comprises:replacement of an aliphatic amino acid with another aliphatic aminoacid; replacement of a Serine with a Threonine or vice versa;replacement of an acidic residue with another acidic residue;replacement of a residue bearing an amide group with another residuebearing an amide group; exchange of a basic residue with another basicresidue; or replacement of an aromatic residue with another aromaticresidue;

(e) the nucleic acid (polynucleotide) of (a), (b), (c) or (d) encoding apolypeptide having a lignocellulosic activity but lacking a signalsequence, a prepro domain, a dockerin domain, and/or a carbohydratebinding module (CBM),

wherein optionally the carbohydrate binding module (CBM) comprises, orconsists of, a cellulose binding module, a lignin binding module, axylose binding module, a mannanse binding module, a xyloglucan-specificmodule and/or a arabinofuranosidase binding module;

(f) the nucleic acid (polynucleotide) of (a), (b), (c), (d) or (e)encoding a polypeptide having a lignocellulosic activity furthercomprising a heterologous sequence;

(g) the nucleic acid (polynucleotide) of (f), wherein the heterologoussequence comprises, or consists of a sequence encoding: (i) aheterologous signal sequence, a heterologous carbohydrate bindingmodule, a heterologous dockerin domain, a heterologous catalytic domain(CD), or a combination thereof; (ii) the sequence of (ii), wherein theheterologous signal sequence, carbohydrate binding module or catalyticdomain (CD) is derived from a heterologous lignocellulosic enzyme; or,(iii) a tag, an epitope, a targeting peptide, a cleavable sequence, adetectable moiety or an enzyme;

(h) the nucleic acid (polynucleotide) of (g), wherein the heterologouscarbohydrate binding module (CBM) comprises, or consists of, a cellulosebinding module, a lignin binding module, a xylose binding module, amannanse binding module, a xyloglucan-specific module and/or aarabinofuranosidase binding module;

(i) the nucleic acid (polynucleotide) of (g), wherein the heterologoussignal sequence targets the encoded protein to a vacuole, theendoplasmic reticulum, a chloroplast or a starch granule; or

(j) a nucleic acid sequence (polynucleotide) fully (completely)complementary to (a), (b), (c), (d), (e), (f), (g), (h) or (i).

2. The isolated, synthetic or recombinant nucleic acid of paragraph[0317], wherein the lignocellulosic activity comprises

(a) a cellulase, a cellulolytic activity or a cellobiohydrolaseactivity, or any combination thereof;

(b) an activity comprising hydrolyzing (degrading) soluble oligomers tofermentable, monomeric sugars;

(c) an activity comprising hydrolyzing (degrading) solublecellooligsaccharides and arabinoxylan oligomers into monomers, andoptionally the monomers comprise xylose, arabinose and glucose;

(d) catalyzing the hydrolysis of (degrading) plant biomasspolysaccharides;

(e) catalyzing the hydrolysis of (degrading) a glucan or lignin toproduce a smaller molecular weight polysaccharides or oligomers ormonomers;

(f) catalyzing hydrolysis of 1,4-beta-D-glycosidic linkages;

(g) an endocellulase activity comprising an endo-1,4-beta-endocellulaseactivity;

(f) a 1,4-beta-D-glycosidic linkage hydrolysis activity comprisinghydrolysis of a 1,4-beta-D-glycosidic linkage in a cellulose, acellulose derivative, a lichenin or a cereal, wherein optionally thecellulose derivative comprises a carboxy methyl cellulose or a hydroxyethyl cellulose, or the cereal comprises a beta-D-glucan or axyloglucan;

(g) catalyzing hydrolysis of glucanase linkages;

(h) catalyzing hydrolysis of β-1,4- and/or β-1,3-glucanase linkages;

(i) catalyzing hydrolysis of endo-glucan linkages;

(j) catalyzing hydrolysis of endo-1,4-beta-D-glucan 4-glucano hydrolaseactivity;

(k) catalyzing hydrolysis of internal endo-β-1,4-glucanase linkagesand/or β-1,3-glucanase linkages;

(l) catalyzing hydrolysis of internal β-1,3-glucosidic linkages;

(m) catalyzing hydrolysis of polysaccharides comprising glucopyranose;

(n) catalyzing hydrolysis of polysaccharides comprising1,4-β-glycoside-linked D-glucopyranoses;

(o) catalyzing hydrolysis of cellulose, a cellulose derivative or ahemicellulose;

(p) the activity of (o), wherein the cellulase activity (hydrolysis ofcellulose, a cellulose derivative or a hemicellulose) compriseshydrolyzing (degrading) a cellulose or a hemicellulose in sugar canebagasse, corn fiber, corn seed fiber, wood, wood waste, wood pulp, paperpulp, a wood product or paper product, a plant biomass, a plant biomasscomprising seeds, grains, tubers, plant wastes or byproducts of food orfeed processing or industrial processing, stalks, corn, cobs, stover,grasses, an Indian grass or a switch grass;

(q) catalyzing hydrolysis of glucan in a feed, a food product or abeverage;

(r) the activity of (q), wherein the feed, food product or beveragecomprises a cereal-based animal feed, a wort or a beer, a dough, a fruitor a vegetable;

(s) catalyzing hydrolysis of a glucan in a microbial cell, a fungalcell, a mammalian cell, a plant cell or any plant material comprising acellulosic part;

(t) the activity of any of (a) to (s), wherein the activity isthermostable or thermotolerant;

(u) the activity of any of (t), wherein activity is stable or tolerantunder conditions comprising a temperature range of between about 37° C.to about 95° C., or between about 55° C. to about 85° C., or betweenabout 70° C. to about 75° C., or between about 70° C. to about 95° C.,or between about 90° C. to about 95° C., or retains a lignocellulosicactivity in a temperature in the range between about 1° C. to about 5°C., between about 5° C. to about 15° C., between about 15° C. to about25° C., between about 25° C. to about 37° C., or between about 37° C. toabout 95° C., 96° C., 97° C., 98° C. or 99° C.;

(v) the activity of any of (t), wherein activity is stable or tolerantafter exposure to a temperature in the range from greater than 37° C. toabout 95° C., from greater than 55° C. to about 85° C., or between about70° C. to about 75° C., or from greater than 90° C. to about 95° C., orafter exposure to a temperature in the range between about 1° C. toabout 5° C., between about 5° C. to about 15° C., between about 15° C.to about 25° C., between about 25° C. to about 37° C., or between about37° C. to about 95° C., 96° C., 97° C., 98° C. or 99° C.; or

(w) the activity of any of (a) to (s), wherein the enzyme is activeunder conditions comprising about pH 6.5, pH 6, pH 5.5, pH 5, pH 4.5 orpH 4 or more acidic; or, under conditions comprising about pH 7, pH 7.5pH 8.0, pH 8.5, pH 9, pH 9.5, pH 10, pH 10.5 or pH 11 or more basic pH.

3. A nucleic acid probe for identifying a nucleic acid encoding apolypeptide with a lignocellulosic activity, wherein the probe comprises

(a) at least 20, 30, 40, 50, 60, 75, 100, 125, 150, or 200 or moreconsecutive bases of the nucleic acid sequence (polynucleotide) ofparagraph [0317], wherein the probe identifies the nucleic acid bybinding or hybridization;

(b) the probe of (a), wherein the probe comprises an oligonucleotidecomprising at least about 10 to 50, about 20 to 60, about 30 to 70,about 40 to 80, about 60 to 100, or about 50 to 150 consecutive bases;

(c) the probe of (a) or (b), wherein the probe comprises consecutivebases of the sequence of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ IDNO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ IDNO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ IDNO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ IDNO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ IDNO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ IDNO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ IDNO:67, SEQ ID NO:69, SEQ ID NO:71, SEQ ID NO:73, SEQ ID NO:75, SEQ IDNO:77, SEQ ID NO:79, SEQ ID NO:81, SEQ ID NO:83, SEQ ID NO:85, SEQ IDNO:87, SEQ ID NO:89, SEQ ID NO:91, SEQ ID NO:93, SEQ ID NO:95, SEQ IDNO:97, SEQ ID NO:99, SEQ ID NO:101, SEQ ID NO:103, SEQ ID NO:105, SEQ IDNO:107, SEQ ID NO:109, SEQ ID NO:111, SEQ ID NO:113, SEQ ID NO:115, SEQID NO:117, SEQ ID NO:119, SEQ ID NO:121, SEQ ID NO:123, SEQ ID NO:125,SEQ ID NO:127, SEQ ID NO:129, SEQ ID NO:131, SEQ ID NO:133, and/or SEQID NO:135;

(d) the probe of (a), (b) or (c) further comprising a detectable agent;or

(e) the probe of (d), wherein the detectable agent comprises aradioactive isotope, a fluorescent dye or an enzyme capable ofcatalyzing the formation of a detectable product.

4. An amplification primer pair for amplifying a nucleic acid encoding apolypeptide having a lignocellulosic activity, wherein the amplificationprimer pair

(a) is capable of amplifying a nucleic acid comprising the nucleic acidsequence of paragraph [0317], or a subsequence thereof;

(b) comprises a first member having a sequence as set forth by about thefirst (the 5′) 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25,26, 27, 28, 29, 30 or more residues of SEQ ID NO:1, etc, and a secondmember having a sequence as set forth by about the first (the 5′) 12,13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30or more residues of the complementary strand of the first member; or

(c) comprises the amplification primer pair or (a) or (b), wherein amember of the amplification primer pair comprises an oligonucleotidecomprising at least about 10 to 50 consecutive bases of the sequence,or, about 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26,27, 28, 29, 30 or more consecutive bases of the sequence.

5. An isolated or recombinant lignocellulosic enzyme-encoding nucleicacid comprising:

(a) a nucleic acid generated by amplification of a polynucleotide usingthe amplification primer pair of paragraph 4;

(b) the nucleic acid of (a), wherein the amplification is by polymerasechain reaction (PCR);

(c) the nucleic acid of (a), wherein the nucleic acid is generated byamplification of a gene library;

(d) the nucleic acid of (c), wherein the gene library is anenvironmental library.

(e) the nucleic acid of (a), (b), (c) or (d) encoding a polypeptidehaving a lignocellulosic activity but lacking a signal sequence, aprepro domain, a dockerin domain, and/or a carbohydrate binding module(CBM),

wherein optionally the carbohydrate binding module (CBM) comprises, orconsists of, a cellulose binding module, a lignin binding module,cellulase or a cellobiohydrolase module; or

(f) the nucleic acid of (a), (b), (c), (d) or (e) encoding a polypeptidehaving a lignocellulosic activity further comprising a heterologoussequence.

6. An isolated, synthetic or recombinant lignocellulosic enzyme encodedby the nucleic acid of paragraph 5.

7. A method of amplifying a nucleic acid encoding a polypeptide having alignocellulosic enzyme activity comprising amplification of a templatenucleic acid with the amplification primer pair of paragraph 4.

8. An expression cassette comprising a nucleic acid comprising thenucleic acid sequence of paragraph 1 or paragraph 5.

9. A vector comprising a nucleic acid comprising the nucleic acidsequence of paragraph 1 or paragraph 5, or the expression cassette ofparagraph 8, wherein optionally the vector comprises an expressionvector or a cloning vector.

10. A cloning vehicle comprising a nucleic acid comprising the nucleicacid sequence of paragraph 1 or paragraph 5, the vector of paragraph 9,or the expression cassette of paragraph 8, wherein optionally thecloning vehicle comprises a viral vector, a plasmid, a phage, aphagemid, a cosmid, a fosmid, a bacteriophage or an artificialchromosome, and optionally the viral vector comprises an adenovirusvector, a retroviral vector or an adeno-associated viral vector, andoptionally the cloning vehicle comprises a bacterial artificialchromosome (BAC), a plasmid, a bacteriophage P1-derived vector (PAC), ayeast artificial chromosome (YAC), or a mammalian artificial chromosome(MAC).

11. A transformed, infected, transformed or host cell comprising

(a) a nucleic acid comprising the nucleic acid sequence of paragraph 1or paragraph 5, or the expression cassette of paragraph 8, the vector ofparagraph 9, or a cloning vehicle of paragraph 10;

(b) the cell of (a), wherein the cell is a bacterial cell, a mammaliancell, a fungal cell, a yeast cell, an insect cell or a plant cell;

(c) the plant cell of (b), wherein the plant cell is derived from aplant of the genera Anacardium, Arachis, Asparagus, Atropa, Avena,Brassica, Citrus, Citrullus, Capsicum, Carthamus, Cocos, Coffea,Cruciferae, Cucumis, Cucurbita, Daucus, Elaeis, Fragaria, Glycine,Gossypium, Helianthus, Heterocallis, Hordeum, Hyoscyamus, Lactuca,Linum, Lolium, Lupinus, Lycopersicon, Malus, Manihot, Majorana,Medicago, Nicotiana, Olea, Oryza, Panieum, Pannisetum, Persea,Phaseolus, Pistachia, Pisum, Pyrus, Prunus, Raphanus, Ricinus, Secale,Senecio, Sinapis, Solanum, Sorghum, Theobromus, Trigonella, Triticum,Vicia, Vitis, Vigna or Zea; or

(d) the plant cell of (b), wherein the plant cell is derived from a cornplant, a sorghum plant, a potato plant, a tomato plant, a wheat plant,an oilseed plant, a rapeseed plant, a soybean plant, a rice plant, abarley plant, a grass, or a tobacco plant.

12. A transgenic non-human animal comprising the nucleic acid sequenceof paragraph 1 or paragraph 5, or the expression cassette of paragraph8, the vector of paragraph 9, or a cloning vehicle of paragraph 10,wherein optionally the transgenic non-human animal is a mouse, rat, pig,cow or goat.

13. A transgenic plant comprising

(a) the nucleic acid sequence of paragraph 1 or paragraph 5, or theexpression cassette of paragraph 8, the vector of paragraph 9, or acloning vehicle of paragraph 10;

(b) the transgenic plant of (a), wherein the plant is a corn plant, asorghum plant, a potato plant, a tomato plant, a wheat plant, an oilseedplant, a rapeseed plant, a soybean plant, a rice plant, a barley plant,a grass, or a tobacco plant; or

(c) the transgenic plant of (a), wherein the plant is of the generaAnacardium, Arachis, Asparagus, Atropa, Avena, Brassica, Citrus,Citrullus, Capsicum, Carthamus, Cocos, Coffea, Cruciferae, Cucumis,Cucurbita, Daucus, Elaeis, Fragaria, Glycine, Gossypium, Helianthus,Heterocallis, Hordeum, Hyoscyamus, Lactuca, Linum, Lolium, Lupinus,Lycopersicon, Malus, Manihot, Majorana, Medicago, Nicotiana, Olea,Oryza, Panieum, Pannisetum, Persea, Phaseolus, Pistachia, Pisum, Pyrus,Prunus, Raphanus, Ricinus, Secale, Senecio, Sinapis, Solanum, Sorghum,Theobromus, Trigonella, Triticum, Vicia, Vitis, Vigna or Zea.

14. A transgenic seed comprising

(a) the nucleic acid sequence of paragraph 1 or paragraph 5, or theexpression cassette of paragraph 8, the vector of paragraph 9, or acloning vehicle of paragraph 10;

(b) the transgenic seed of (a), wherein the seed is a corn seed, a wheatkernel, an oilseed, a rapeseed, a soybean seed, a palm kernel, asunflower seed, a sesame seed, a rice, a barley, a peanut or a tobaccoplant seed; or

(c) the transgenic seed of (a), wherein the seed is derived from a plantof the genera Anacardium, Arachis, Asparagus, Atropa, Avena, Brassica,Citrus, Citrullus, Capsicum, Carthamus, Cocos, Coffea, Cruciferae,Cucumis, Cucurbita, Daucus, Elaeis, Fragaria, Glycine, Gossypium,Helianthus, Heterocallis, Hordeum, Hyoscyamus, Lactuca, Linum, Lolium,Lupinus, Lycopersicon, Malus, Manihot, Majorana, Medicago, Nicotiana,Olea, Oryza, Panieum, Pannisetum, Persea, Phaseolus, Pistachia, Pisum,Pyrus, Prunus, Raphanus, Ricinus, Secale, Senecio, Sinapis, Solanum,Sorghum, Theobromus, Trigonella, Triticum, Vicia, Vitis, Vigna or Zea.

15. An antisense oligonucleotide comprising a nucleic acid sequencecomplementary to or capable of hybridizing under stringent conditions tothe nucleic acid sequence of paragraph 1 or paragraph 5, whereinoptionally the antisense oligonucleotide has a length of between about10 to 50, about 20 to 60, about 30 to 70, about 40 to 80, or about 60 to100 bases, wherein optionally the antisense oligonucleotide comprises anRNAi, miRNA, iRNA, or a ribozyme.

16. A method of inhibiting the translation of an enzyme message in acell comprising administering to the cell or expressing in the cell anantisense oligonucleotide comprising a nucleic acid sequencecomplementary to or capable of hybridizing under stringent conditions tothe nucleic acid sequence of paragraph 1 or paragraph 5.

17. A double-stranded interference RNA (RNAi) molecule comprising asubsequence of the nucleic acid sequence of paragraph 1, whereinoptionally the RNAi comprises an siRNA or an miRNA, and optionally theRNAi molecule is about 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22,23, 24, 25, 26 or more duplex nucleotides in length.

18. A method of inhibiting the expression of a lignocellulosic enzyme ormessage (mRNA) in a cell comprising administering to the cell orexpressing in the cell a double-stranded interference RNA (RNAi)molecule as set forth in paragraph 17.

19. An isolated, synthetic or recombinant polypeptide comprising

(a) an amino acid sequence having at least 50%, 51%, 52%, 53%, 54%, 55%,56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%,70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%,84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%,98%, 99%, or more, or complete (100%) sequence identity to SEQ ID NO:2,SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ IDNO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ IDNO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ IDNO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ IDNO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ IDNO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:72, SEQ IDNO:74, SEQ ID NO:76, SEQ ID NO:78, SEQ ID NO:80, SEQ ID NO:82, SEQ IDNO:84, SEQ ID NO:86, SEQ ID NO:88, SEQ ID NO:90, SEQ ID NO:92, SEQ IDNO:94, SEQ ID NO:96, SEQ ID NO:98, SEQ ID NO:100, SEQ ID NO:102, SEQ IDNO:104, SEQ ID NO:106, SEQ ID NO:108, SEQ ID NO:110, SEQ ID NO:112, SEQID NO:114, SEQ ID NO:116, SEQ ID NO:118, SEQ ID NO:120, SEQ ID NO:122,SEQ ID NO:124, SEQ ID NO:126, SEQ ID NO:128, SEQ ID NO:130, SEQ IDNO:132, SEQ ID NO:134, and/or SEQ ID NO:136, or enzymatically activesubsequences (fragments) thereof, over a region of at least about 20,25, 30, 35, 40, 45, 50, 55, 60, 75, 100, 150, 200, 250, 300 or moreresidues, or over the full length of the polypeptide or enzyme,

wherein the nucleic acid encodes a polypeptide having a lignocellulosicactivity, and optionally the lignocellulosic activity comprises acellulase, a cellulolytic activity, an endoglucanase or acellobiohydrolase activity,

wherein optionally the sequence identities are determined by analysiswith a sequence comparison algorithm or by a visual inspection, andoptionally the sequence comparison algorithm is a BLAST version 2.2.2algorithm where a filtering setting is set to blastall -p blastp -d “nrpataa”-F F, and all other options are set to default;

(b) an amino acid sequence encoded by the nucleic acid of paragraph 1,wherein the polypeptide has (i) a lignocellulosic activity, andoptionally the lignocellulosic activity comprises a cellulase, acellulolytic activity, an endoglucanase or a cellobiohydrolase activity,or, (ii) has immunogenic activity in that it is capable of generating anantibody that specifically binds to a polypeptide having the sequence ofSEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ IDNO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ IDNO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ IDNO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ IDNO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ IDNO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ IDNO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ IDNO:72, SEQ ID NO:74, SEQ ID NO:76, SEQ ID NO:78, SEQ ID NO:80, SEQ IDNO:82, SEQ ID NO:84, SEQ ID NO:86, SEQ ID NO:88, SEQ ID NO:90, SEQ IDNO:92, SEQ ID NO:94, SEQ ID NO:96, SEQ ID NO:98, SEQ ID NO:100, SEQ IDNO:102, SEQ ID NO:104, SEQ ID NO:106, SEQ ID NO:108, SEQ ID NO:110, SEQID NO:112, SEQ ID NO:114, SEQ ID NO:116, SEQ ID NO:118, SEQ ID NO:120,SEQ ID NO:122, SEQ ID NO:124, SEQ ID NO:126, SEQ ID NO:128, SEQ IDNO:130, SEQ ID NO:132, SEQ ID NO:134, and/or SEQ ID NO:136, and/orenzymatically active subsequences (fragments) thereof;

(c) the amino acid sequence of (a) or (b), and comprising at least oneamino acid residue conservative substitution,

(d) the amino acid sequence of (c), wherein the conservativesubstitution comprises replacement of an aliphatic amino acid withanother aliphatic amino acid; replacement of a serine with a threonineor vice versa; replacement of an acidic residue with another acidicresidue; replacement of a residue bearing an amide group with anotherresidue bearing an amide group; exchange of a basic residue with anotherbasic residue; or, replacement of an aromatic residue with anotheraromatic residue, or a combination thereof,

and optionally the aliphatic residue comprises Alanine, Valine, Leucine,Isoleucine or a synthetic equivalent thereof; the acidic residuecomprises Aspartic acid, Glutamic acid or a synthetic equivalentthereof; the residue comprising an amide group comprises Aspartic acid,Glutamic acid or a synthetic equivalent thereof; the basic residuecomprises Lysine, Arginine or a synthetic equivalent thereof; or, thearomatic residue comprises Phenylalanine, Tyrosine or a syntheticequivalent thereof;

(e) the polypeptide of (a), (b), (c) or (d) having a lignocellulosicactivity but lacking a signal sequence, a prepro domain, a dockerindomain, and/or a carbohydrate binding module (CBM),

wherein optionally the carbohydrate binding module (CBM) comprises, orconsists of, a cellulose binding module, a lignin binding module, axylose binding module, a mannanse binding module, a xyloglucan-specificmodule and/or a arabinofuranosidase binding module;

(f) the polypeptide of (a), (b), (c), (d) or (e) having alignocellulosic activity further comprising a heterologous sequence;

(g) the polypeptide of (f), wherein the heterologous sequence comprises,or consists of: (i) a heterologous signal sequence, a heterologouscarbohydrate binding module, a heterologous dockerin domain, aheterologous catalytic domain (CD), or a combination thereof; (ii) thesequence of (ii), wherein the heterologous signal sequence, carbohydratebinding module or catalytic domain (CD) is derived from a heterologouslignocellulosic enzyme; and/or, (iii) a tag, an epitope, a targetingpeptide, a cleavable sequence, a detectable moiety or an enzyme;

(h) the polypeptide of (g), wherein the heterologous carbohydratebinding module (CBM) comprises, or consists of, a cellulose bindingmodule, a lignin binding module, a xylose binding module, a mannansebinding module, a xyloglucan-specific module and/or aarabinofuranosidase binding module; or

(i) polypeptide of (g), wherein the heterologous signal sequence targetsthe encoded protein to a vacuole, the endoplasmic reticulum, achloroplast or a starch granule.

20. The isolated, synthetic or recombinant polypeptide of paragraph 19,or the lignocellulosic enzyme of paragraph 6, wherein thelignocellulosic activity comprises

(a) a cellulase, a cellulolytic activity, an endoglucanase or acellobiohydrolase activity, or any combination thereof;

(b) an activity comprising hydrolyzing (degrading) soluble oligomers tofermentable, monomeric sugars;

(c) an activity comprising hydrolyzing (degrading) solublecellooligsaccharides and arabinoxylan oligomers into monomers, andoptionally the monomers comprise xylose, arabinose and glucose;

(d) catalyzing the hydrolysis of (degrading) plant biomasspolysaccharides;

(e) catalyzing the hydrolysis of (degrading) a glucan or lignin toproduce a smaller molecular weight polysaccharides or oligomers ormonomers;

(f) catalyzing hydrolysis of 1,4-beta-D-glycosidic linkages;

(g) an endocellulase activity comprising an endo-1,4-beta-endocellulaseactivity;

(f) a 1,4-beta-D-glycosidic linkage hydrolysis activity comprisinghydrolysis of a 1,4-beta-D-glycosidic linkage in a cellulose, acellulose derivative, a lichenin or a cereal, wherein optionally thecellulose derivative comprises a carboxy methyl cellulose or a hydroxyethyl cellulose, or the cereal comprises a beta-D-glucan or axyloglucan;

(g) catalyzing hydrolysis of glucanase linkages;

(h) catalyzing hydrolysis of β-1,4- and/or β-1,3-glucanase linkages;

(i) catalyzing hydrolysis of endo-glucan linkages;

(j) catalyzing hydrolysis of endo-1,4-beta-D-glucan 4-glucano hydrolaseactivity;

(k) catalyzing hydrolysis of internal endo-β-1,4-glucanase linkagesand/or β-1,3-glucanase linkages;

(l) catalyzing hydrolysis of internal β-1,3-glucosidic linkages;

(m) catalyzing hydrolysis of polysaccharides comprising glucopyranose;

(n) catalyzing hydrolysis of polysaccharides comprising1,4-β-glycoside-linked D-glucopyranoses;

(o) catalyzing hydrolysis of cellulose, a cellulose derivative or ahemicellulose;

(p) the activity of (o), wherein the enzymatic activity compriseshydrolyzing (degrading) a cellulose or a hemicellulose in sugar canebagasse, corn fiber, corn seed fiber, wood, wood pulp, paper pulp, awood product, wood waste or paper product, a plant biomass, a plantbiomass comprising seeds, grains, tubers, plant wastes or byproducts offood or feed processing or industrial processing, stalks, corn, cobs,stover, grasses, an Indian grass or a switch grass;

(q) catalyzing hydrolysis of glucan in a feed, a food product or abeverage;

(r) the activity of (q), wherein the feed, food product or beveragecomprises a cereal-based animal feed, a wort or a beer, a dough, a fruitor a vegetable;

(s) catalyzing hydrolysis of a glucan in a microbial cell, a fungalcell, a mammalian cell, a plant cell or any plant material comprising acellulosic part;

(t) the activity of any of (a) to (s), wherein the activity isthermostable or thermotolerant;

(u) the activity of any of (t), wherein activity is stable or tolerantunder conditions comprising a temperature range of between about 37° C.to about 95° C., or between about 55° C. to about 85° C., or betweenabout 70° C. to about 75° C., or between about 70° C. to about 95° C.,or between about 90° C. to about 95° C., or retains a lignocellulosicactivity in a temperature in the range between about 1° C. to about 5°C., between about 5° C. to about 15° C., between about 15° C. to about25° C., between about 25° C. to about 37° C., or between about 37° C. toabout 95° C., 96° C., 97° C., 98° C. or 99° C.;

(v) the activity of any of (t), wherein activity is stable or tolerantafter exposure to a temperature in the range from greater than 37° C. toabout 95° C., from greater than 55° C. to about 85° C., or between about70° C. to about 75° C., or from greater than 90° C. to about 95° C., orafter exposure to a temperature in the range between about 1° C. toabout 5° C., between about 5° C. to about 15° C., between about 15° C.to about 25° C., between about 25° C. to about 37° C., or between about37° C. to about 95° C., 96° C., 97° C., 98° C. or 99° C.; or

(w) the activity of any of (a) to (s), wherein the enzyme is activeunder conditions comprising about pH 6.5, pH 6, pH 5.5, pH 5, pH 4.5 orpH 4 or more acidic; or, under conditions comprising about pH 7, pH 7.5pH 8.0, pH 8.5, pH 9, pH 9.5, pH 10, pH 10.5 or pH 11 or more basic pH.

21. The isolated, synthetic or recombinant polypeptide of paragraph 19,or the lignocellulosic enzyme of paragraph 6, wherein the polypeptide orenzyme comprises at least one glycosylation site, and optionally theglycosylation is an N-linked glycosylation, and optionally thepolypeptide is glycosylated after being expressed in a Pichia, e.g., aPichia pastoris, a Schizosaccharomyces, e.g., a Schizosaccharomycespombe, and/or a Pseudomonas, e.g., a Pseudomonas fluorescens.

22. A protein preparation comprising the polypeptide of paragraph 19, orthe lignocellulosic enzyme of paragraph 6, wherein the proteinpreparation comprises a liquid, a solid or a gel.

23. A heterodimer comprising the polypeptide of paragraph 19, or thelignocellulosic enzyme of paragraph 6, and a second domain, whereinoptionally the second domain comprises a polypeptide and the heterodimeris a fusion protein, and optionally the second domain comprises anepitope, a heterologous enzyme, a detectable protein or peptide, animmunogenic protein or peptide or a tag.

24. A homodimer comprising the polypeptide of paragraph 19 or thelignocellulosic enzyme of paragraph 6.

25. An immobilized polypeptide or enzyme, or an immobilized nucleicacid, wherein the polypeptide comprises the sequence of paragraph 19, orthe lignocellulosic enzyme of paragraph 6, or the nucleic acid comprisesthe nucleic acid sequence of paragraph 1 or paragraph 5, or the probe ofparagraph 3, wherein optionally the polypeptide or nucleic acid isimmobilized on a cell, a metal, a resin, a polymer, a ceramic, a glass,a microelectrode, a graphitic particle, a bead, a gel, a plate, an arrayor a capillary tube.

26. An array comprising the immobilized polypeptide or immobilizednucleic acid of paragraph 25.

27. An isolated, synthetic or recombinant antibody that specificallybinds to the polypeptide of paragraph 19, wherein optionally theantibody is a monoclonal or a polyclonal antibody.

28. A hybridoma comprising an antibody that specifically binds to thepolypeptide of paragraph 19.

29. A method of isolating or identifying a polypeptide with alignocellulosic activity comprising the steps of:

(a) providing the antibody of paragraph 27;

(b) providing a sample comprising polypeptides; and

(c) contacting the sample of step (b) with the antibody of step (a)under conditions wherein the antibody can specifically bind to thepolypeptide, thereby isolating or identifying a polypeptide having alignocellulosic activity.

30. A method of making an anti-cellulase or an anti-lignocellulosicenzyme antibody comprising (a) administering to a non-human animal thenucleic acid of paragraph 1 or paragraph 5 in an amount sufficient togenerate a humoral immune response, thereby making ananti-lignocellulosic enzyme or an anti-cellulase antibody, or

(b) administering to a non-human animal the polypeptide of paragraph 19in an amount sufficient to generate a humoral immune response, therebymaking an anti-lignocellulosic enzyme or an anti-cellulase antibody.

31. A method of producing a recombinant polypeptide comprising:

(A) (a) providing a nucleic acid operably linked to a promoter, whereinthe nucleic acid comprises the nucleic acid sequence of paragraph 1 orparagraph 5; and

(b) expressing the nucleic acid of step (a) under conditions that allowexpression of the polypeptide, thereby producing a recombinantpolypeptide; or

(B) the method of (A), wherein the method further comprises transforminga host cell with the nucleic acid of step (a) followed by expressing thenucleic acid of step (a), thereby producing a recombinant polypeptide ina transformed cell; or

(C) the method of (A) or (B), wherein the promoter is or comprises: aviral, bacterial, mammalian or plant promoter; or, a plant promoter; or,a potato, rice, corn, wheat, tobacco or barley promoter; or, aconstitutive promoter or a CaMV35S promoter; or, an inducible promoter;or, a tissue-specific promoter or an environmentally regulated or adevelopmentally regulated promoter; or, a seed-specific, aleaf-specific, a root-specific, a stem-specific or an abscission-inducedpromoter; or, a seed preferred promoter, a maize gamma zein promoter ora maize ADP-gpp promoter.

32. A method for identifying a polypeptide having a lignocellulosicactivity comprising the following steps:

(a) providing the polypeptide of paragraph 19, or the lignocellulosicenzyme of paragraph 6;

(b) providing a substrate for a lignocellulosic enzyme; and

(c) contacting the polypeptide with the substrate of step (b) anddetecting a decrease in the amount of substrate or an increase in theamount of a reaction product, wherein a decrease in the amount of thesubstrate or an increase in the amount of the reaction product detects apolypeptide having a lignocellulosic activity.

33. A method for identifying an lignocellulosic enzyme substratecomprising the following steps:

(a) providing the polypeptide of paragraph 19;

(b) providing a test substrate; and

(c) contacting the polypeptide of step (a) with the test substrate ofstep (b) and detecting a decrease in the amount of substrate or anincrease in the amount of reaction product, wherein a decrease in theamount of the substrate or an increase in the amount of a reactionproduct identifies the test substrate as a lignocellulosic enzymesubstrate.

34. A method of determining whether a test compound specifically bindsto a polypeptide comprising the following steps:

(a) expressing a nucleic acid or a vector comprising the nucleic acidunder conditions permissive for translation of the nucleic acid to apolypeptide, wherein the nucleic acid has the nucleic acid sequence ofparagraph 1 or paragraph 5;

(b) providing a test compound;

(c) contacting the polypeptide with the test compound; and

(d) determining whether the test compound of step (b) specifically bindsto the polypeptide.

35. A method of determining whether a test compound specifically bindsto a polypeptide comprising the following steps:

(a) providing the polypeptide of paragraph 19;

(b) providing a test compound;

(c) contacting the polypeptide with the test compound; and

(d) determining whether the test compound of step (b) specifically bindsto the polypeptide.

36. A method for identifying a modulator of a lignocellulosic activitycomprising the following steps:

(a) providing the polypeptide of paragraph 19;

(b) providing a test compound;

(c) contacting the polypeptide of step (a) with the test compound ofstep (b) and measuring an activity of the lignocellulosic enzyme,wherein a change in the lignocellulosic enzyme activity measured in thepresence of the test compound compared to the activity in the absence ofthe test compound provides a determination that the test compoundmodulates the lignocellulosic enzyme activity.

37. The method of paragraph 97, wherein the lignocellulosic enzymeactivity is measured by providing a lignocellulosic enzyme substrate anddetecting a decrease in the amount of the substrate or an increase inthe amount of a reaction product, or, an increase in the amount of thesubstrate or a decrease in the amount of a reaction product,

wherein optionally a decrease in the amount of the substrate or anincrease in the amount of the reaction product with the test compound ascompared to the amount of substrate or reaction product without the testcompound identifies the test compound as an activator of alignocellulosic activity,

and optionally an increase in the amount of the substrate or a decreasein the amount of the reaction product with the test compound as comparedto the amount of substrate or reaction product without the test compoundidentifies the test compound as an inhibitor of a lignocellulosicactivity.

38. A computer system comprising a processor and a data storage devicewherein said data storage device has stored thereon a polypeptidesequence or a nucleic acid sequence, wherein the polypeptide sequencecomprises sequence as set forth in paragraph 19, a polypeptide encodedby the nucleic acid of paragraph 1 or paragraph 5,

wherein optionally the method further comprises a sequence comparisonalgorithm and a data storage device having at least one referencesequence stored thereon, or further comprises an identifier thatidentifies one or more features in said sequence

and optionally the sequence comparison algorithm comprises a computerprogram that indicates polymorphisms.

39. A computer readable medium having stored thereon a polypeptidesequence or a nucleic acid sequence, wherein the polypeptide sequencecomprises the polypeptide of paragraph 19, or a polypeptide encoded bythe nucleic acid of paragraph 1 or paragraph 5.

40. A method for identifying a feature in a sequence comprising thesteps of: (a) reading the sequence using a computer program whichidentifies one or more features in a sequence, wherein the sequencecomprises a polypeptide sequence or a nucleic acid sequence, wherein thepolypeptide sequence comprises the polypeptide of paragraph 19; apolypeptide encoded by the nucleic acid of paragraph 1 or paragraph 5;and (b) identifying one or more features in the sequence with thecomputer program.

41. A method for comparing a first sequence to a second sequencecomprising the steps of: (a) reading the first sequence and the secondsequence through use of a computer program which compares sequences,wherein the first sequence comprises a polypeptide sequence or a nucleicacid sequence, wherein the polypeptide sequence comprises thepolypeptide of paragraph 19 or a polypeptide encoded by the nucleic acidof paragraph 1 or paragraph 5; and (b) determining differences betweenthe first sequence and the second sequence with the computer program.

wherein optionally the method further comprises a step of determiningdifferences between the first sequence and the second sequence, oroptionally the method further comprises the step of identifyingpolymorphisms, or optionally the method further comprises use of anidentifier that identifies one or more features in a sequence,

and optionally the method comprises reading the first sequence using acomputer program and identifying one or more features in the sequence.

42. A method for isolating or recovering a nucleic acid encoding apolypeptide with a lignocellulosic activity from a sample comprising thesteps of:

(a) providing the amplification primer pair of paragraph 4;

(b) isolating a nucleic acid from the sample or treating the sample suchthat nucleic acid in the sample is accessible for hybridization to theamplification primer pair; and,

(c) combining the nucleic acid of step (b) with the amplification primerpair of step (a) and amplifying nucleic acid from the sample, therebyisolating or recovering a nucleic acid encoding a polypeptide with alignocellulosic activity from a sample;

wherein optionally the sample is an environmental sample, or optionallythe sample comprises a water sample, a liquid sample, a soil sample, anair sample or a biological sample, and optionally the biological sampleis derived from a bacterial cell, a protozoan cell, an insect cell, ayeast cell, a plant cell, a fungal cell or a mammalian cell.

43. A method for isolating or recovering a nucleic acid encoding apolypeptide with a lignocellulosic activity from a sample comprising thesteps of:

(a) providing a polynucleotide probe comprising, or consisting of, thenucleic acid sequence of paragraph 1, or the probe of paragraph 3;

(b) isolating a nucleic acid from the sample or treating the sample suchthat nucleic acid

(c) combining the isolated nucleic acid or the treated sample of step(b) with the polynucleotide probe of step (a); and

(d) isolating a nucleic acid that specifically hybridizes with thepolynucleotide probe of step (a), thereby isolating or recovering anucleic acid encoding a polypeptide with a lignocellulosic activity froman sample;

wherein optionally the sample is an environmental sample, or optionallythe sample comprises a water sample, a liquid sample, a soil sample, anair sample or a biological sample, and optionally the biological sampleis derived from a bacterial cell, a protozoan cell, an insect cell, ayeast cell, a plant cell, a fungal cell or a mammalian cell.

44. A method of generating a variant of a nucleic acid encoding apolypeptide with a lignocellulosic activity comprising the steps of:

(a) providing a template nucleic acid comprising the nucleic acidsequence of paragraph 1 or paragraph 5; and

(b) modifying, deleting or adding one or more nucleotides in thetemplate sequence, or a combination thereof, to generate a variant ofthe template nucleic acid

wherein optionally the method further comprises expressing the variantnucleic acid to generate a variant polypeptide with a lignocellulosicactivity,

and optionally the modifications, additions or deletions are introducedby a method comprising error-prone PCR, shuffling,oligonucleotide-directed mutagenesis, assembly PCR, sexual PCRmutagenesis, in vivo mutagenesis, cassette mutagenesis, recursiveensemble mutagenesis, exponential ensemble mutagenesis, site-specificmutagenesis, GeneReassembly, Gene Site Saturation Mutagenesis (GSSM),Tailored Multi-Site Combinatorial Assembly, recursive sequencerecombination, phosphothioate-modified DNA mutagenesis,uracil-containing template mutagenesis, gapped duplex mutagenesis, pointmismatch repair mutagenesis, repair-deficient host strain mutagenesis,chemical mutagenesis, radiogenic mutagenesis, deletion mutagenesis,restriction-selection mutagenesis, restriction-purification mutagenesis,artificial gene synthesis, ensemble mutagenesis, chimeric nucleic acidmultimer creation and a combination thereof

and optionally the method is iteratively repeated until alignocellulosic enzyme having an altered or different activity or analtered or different stability from that of a polypeptide encoded by thetemplate nucleic acid is produced.

45. The method of paragraph 44, wherein

(A) the variant lignocellulosic enzyme: (a) is thermotolerant, andretains some activity after being exposed to an elevated temperature;(b) has increased glycosylation as compared to the lignocellulosicenzyme encoded by a template nucleic acid; or, (c) has a lignocellulosicactivity under a high temperature, wherein the lignocellulosic enzymeencoded by the template nucleic acid is not active under the hightemperature; or

(B) the method is iteratively repeated until (a) a lignocellulosicenzyme-coding sequence having an altered codon usage from that of thetemplate nucleic acid is produced, or, (b) a lignocellulosic enzyme genehaving higher or lower level of message expression or stability fromthat of the template nucleic acid is produced.

46. A method for modifying codons in a nucleic acid encoding apolypeptide with a lignocellulosic activity to increase its expressionin a host cell, the method comprising the following steps:

(a) providing a nucleic acid encoding a polypeptide with alignocellulosic activity comprising the nucleic acid sequence ofparagraph 1 or paragraph 5; and,

(b) identifying a non-preferred or a less preferred codon in the nucleicacid of step (a) and replacing it with a preferred or neutrally usedcodon encoding the same amino acid as the replaced codon, wherein apreferred codon is a codon over-represented in coding sequences in genesin the host cell and a non-preferred or less preferred codon is a codonunder-represented in coding sequences in genes in the host cell, therebymodifying the nucleic acid to increase its expression in a host cell.

47. A method for modifying codons in a nucleic acid encoding alignocellulosic enzyme, the method comprising the following steps:

(a) providing a nucleic acid encoding a polypeptide with alignocellulosic activity comprising the nucleic acid sequence ofparagraph 1 or paragraph 5; and,

(b) identifying a codon in the nucleic acid of step (a) and replacing itwith a different codon encoding the same amino acid as the replacedcodon, thereby modifying codons in a nucleic acid encoding alignocellulosic enzyme.

48. A method for modifying codons in a nucleic acid encoding alignocellulosic enzyme to increase its expression in a host cell, themethod comprising the following steps:

(a) providing a nucleic acid encoding a lignocellulosic enzymecomprising the nucleic

(b) identifying a non-preferred or a less preferred codon in the nucleicacid of step (a) and replacing it with a preferred or neutrally usedcodon encoding the same amino acid as the replaced codon, wherein apreferred codon is a codon over-represented in coding sequences in genesin the host cell and a non-preferred or less preferred codon is a codonunder-represented in coding sequences in genes in the host cell, therebymodifying the nucleic acid to increase its expression in a host cell.

49. A method for modifying a codon in a nucleic acid encoding apolypeptide having a lignocellulosic activity to decrease its expressionin a host cell, the method comprising the following steps:

(a) providing a nucleic acid encoding a lignocellulosic enzymecomprising the nucleic acid sequence of paragraph 1 or paragraph 5; and

(b) identifying at least one preferred codon in the nucleic acid of step(a) and replacing it with a non-preferred or less preferred codonencoding the same amino acid as the replaced codon, wherein a preferredcodon is a codon over-represented in coding sequences in genes in a hostcell and a non-preferred or less preferred codon is a codonunder-represented in coding sequences in genes in the host cell, therebymodifying the nucleic acid to decrease its expression in a host cell,

wherein optionally the host cell is a bacterial cell, a fungal cell, aninsect cell, a yeast cell, a plant cell or a mammalian cell.

50. A method for producing a library of nucleic acids encoding aplurality of modified lignocellulosic enzyme active sites or substratebinding sites, wherein the modified active sites or substrate bindingsites are derived from a first nucleic acid comprising a sequenceencoding a first active site or a first substrate binding site themethod comprising the following steps:

(a) providing a first nucleic acid encoding a first active site or firstsubstrate binding site, wherein the first nucleic acid sequencecomprises a sequence that hybridizes under stringent conditions to thenucleic acid sequence (polynucleotide) of paragraph 1, and the nucleicacid encodes a lignocellulosic enzyme active site or a lignocellulosicenzyme substrate binding site;

(b) providing a set of mutagenic oligonucleotides that encodenaturally-occurring amino acid variants at a plurality of targetedcodons in the first nucleic acid; and,

(c) using the set of mutagenic oligonucleotides to generate a set ofactive site-encoding or substrate binding site-encoding variant nucleicacids encoding a range of amino acid variations at each amino acid codonthat was mutagenized, thereby producing a library of nucleic acidsencoding a plurality of modified lignocellulosic enzyme active sites orsubstrate binding sites.

wherein optionally a mutagenic oligonucleotide or a variant nucleic acidis generated by a method comprising an optimized directed evolutionsystem, Gene Site Saturation Mutagenesis (GSSM), GeneReassembly,Tailored Multi-Site Combinatorial Assembly, error-prone PCR, shuffling,oligonucleotide-directed mutagenesis, assembly PCR, sexual PCRmutagenesis, in vivo mutagenesis, cassette mutagenesis, recursiveensemble mutagenesis, exponential ensemble mutagenesis, site-specificmutagenesis, recursive sequence recombination, phosphothioate-modifiedDNA mutagenesis, uracil-containing template mutagenesis, gapped duplexmutagenesis, point mismatch repair mutagenesis, repair-deficient hoststrain mutagenesis, chemical mutagenesis, radiogenic mutagenesis,deletion mutagenesis, restriction-selection mutagenesis,restriction-purification mutagenesis, artificial gene synthesis,ensemble mutagenesis, chimeric nucleic acid multimer creation and acombination thereof.

51. A method for making a small molecule comprising the following steps:

(a) providing a plurality of biosynthetic enzymes capable ofsynthesizing or modifying a small molecule, wherein one of the enzymescomprises a lignocellulosic enzyme encoded by a nucleic acid comprisingthe nucleic acid sequence of paragraph 1 or paragraph 5;

(b) providing a substrate for at least one of the enzymes of step (a);and

(c) reacting the substrate of step (b) with the enzymes under conditionsthat facilitate a plurality of biocatalytic reactions to generate asmall molecule by a series of biocatalytic reactions.

52. A method for modifying a small molecule comprising the followingsteps:

(a) providing a lignocellulosic enzyme, wherein the enzyme comprises thepolypeptide of paragraph 19, or a polypeptide encoded by a nucleic acidsequence comprising the sequence of paragraph 1 or paragraph 5;

(b) providing a small molecule; and

(c) reacting the enzyme of step (a) with the small molecule of step (b)under conditions that facilitate an enzymatic reaction catalyzed by thelignocellulosic enzyme, thereby modifying a small molecule by alignocellulosic enzymatic reaction.

wherein optionally step (b) comprises providing a plurality of smallmolecule substrates for the enzyme of step (a), thereby generating alibrary of modified small molecules produced by at least one enzymaticreaction catalyzed by the lignocellulosic enzyme;

and optionally the method further comprises providing a plurality ofadditional enzymes under conditions that facilitate a plurality ofbiocatalytic reactions by the enzymes to form a library of modifiedsmall molecules produced by the plurality of enzymatic reactions;

and optionally the method further comprises the step of testing thelibrary to determine if a particular modified small molecule whichexhibits a desired activity is present within the library, whereinoptionally the step of testing the library further comprises the stepsof systematically eliminating all but one of the biocatalytic reactionsused to produce a portion of the plurality of the modified smallmolecules within the library by testing the portion of the modifiedsmall molecule for the presence or absence of the particular modifiedsmall molecule with a desired activity, and identifying at least onespecific biocatalytic reaction that produces the particular modifiedsmall molecule of desired activity.

53. A method for determining a functional fragment of a lignocellulosicenzyme comprising the steps of:

(a) providing a lignocellulosic enzyme, wherein the enzyme comprises thepolypeptide of paragraph 19, or a polypeptide encoded by the nucleicacid of paragraph 1 or paragraph 5; and

(b) deleting a plurality of amino acid residues from the sequence ofstep (a) and testing the remaining subsequence for a lignocellulosicactivity, thereby determining a functional fragment of a lignocellulosicenzyme.

wherein optionally the lignocellulosic enzyme activity is measured byproviding a lignocellulosic enzyme substrate and detecting a decrease inthe amount of the substrate or an increase in the amount of a reactionproduct.

54. A method for whole cell engineering of new or modified phenotypes byusing real-time metabolic flux analysis, the method comprising thefollowing steps:

(a) making a modified cell by modifying the genetic composition of acell, wherein the genetic composition is modified by addition to thecell of a nucleic acid comprising the nucleic acid sequence of paragraph1 or paragraph 5;

(b) culturing the modified cell to generate a plurality of modifiedcells;

(c) measuring at least one metabolic parameter of the cell by monitoringthe cell culture of step (b) in real time; and,

(d) analyzing the data of step (c) to determine if the measuredparameter differs from a comparable measurement in an unmodified cellunder similar conditions, thereby identifying an engineered phenotype inthe cell using real-time metabolic flux analysis.

wherein optionally the genetic composition of the cell is modified by amethod comprising deletion of a sequence or modification of a sequencein the cell, or, knocking out the expression of a gene,

and optionally the method further comprises selecting a cell comprisinga newly engineered phenotype,

and optionally the method further comprises culturing the selected cell,thereby generating a new cell strain comprising a newly engineeredphenotype.

55. An isolated, synthetic or recombinant signal (or leader) sequence(signal peptide (SP)) consisting of an amino acid sequence as set forthin the amino terminal residues 1 to 12, 1 to 13, 1 to 14, 1 to 15, 1 to16, 1 to 17, 1 to 18, 1 to 19, 1 to 20, 1 to 21, 1 to 22, 1 to 23, 1 to24, 1 to 25, 1 to 26, 1 to 27, 1 to 28, 1 to 28, 1 to 30, 1 to 31, 1 to32, 1 to 33, 1 to 34, 1 to 35, 1 to 36, 1 to 37, 1 to 38, 1 to 40, 1 to41, 1 to 42, 1 to 43 or 1 to 44, of (a) an amino acid sequence as setforth in paragraph 19; or, (b) an amino acid sequence as set forth inSEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ IDNO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ IDNO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ IDNO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ IDNO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ IDNO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ IDNO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ IDNO:72, SEQ ID NO:74, SEQ ID NO:76, SEQ ID NO:78, SEQ ID NO:80, SEQ IDNO:82, SEQ ID NO:84, SEQ ID NO:86, SEQ ID NO:88, SEQ ID NO:90, SEQ IDNO:92, SEQ ID NO:94, SEQ ID NO:96, SEQ ID NO:98, SEQ ID NO:100, SEQ IDNO:102, SEQ ID NO:104, SEQ ID NO:106, SEQ ID NO:108, SEQ ID NO:110, SEQID NO:112, SEQ ID NO:114, SEQ ID NO:116, SEQ ID NO:118, SEQ ID NO:120,SEQ ID NO:122, SEQ ID NO:124, SEQ ID NO:126, SEQ ID NO:128, SEQ IDNO:130, SEQ ID NO:132, SEQ ID NO:134, and/or SEQ ID NO:136, and/orenzymatically active subsequences (fragments) thereof.

56. A chimeric polypeptide comprising at least a first domain comprisinga signal sequence (signal peptide (SP)) or leader sequence having theamino acid sequence of paragraph 55, and at least a second domaincomprising a heterologous polypeptide or peptide, wherein theheterologous polypeptide or peptide is not naturally associated with thesignal peptide (SP) or leader sequence,

and optionally the heterologous polypeptide or peptide is not alignocellulosic enzyme, and optionally the heterologous polypeptide orpeptide is amino terminal to, carboxy terminal to or on both ends of thesignal peptide (SP) or leader sequence.

57. An isolated, synthetic or recombinant nucleic acid encoding achimeric polypeptide, wherein the chimeric polypeptide comprises atleast a first domain comprising signal peptide (SP) or leader sequencehaving the amino acid sequence of paragraph 55 and at least a seconddomain comprising a heterologous polypeptide or peptide, wherein theheterologous polypeptide or peptide is not naturally associated with thesignal peptide (SP) or leader sequence.

58. An isolated, synthetic or recombinant nucleic acid comprising: (a) asequence encoding a polypeptide having a lignocellulosic activity and aheterologous signal (or leader) sequence (signal peptide (SP)), whereinthe nucleic acid comprises the nucleic acid sequence of paragraph 1 orparagraph 5; (b) the sequence of (a) wherein the signal (or leader)sequence (signal peptide (SP)) is derived from another lignocellulosicenzyme or a non-lignocellulosic enzyme; or, (c) the sequence of (a)wherein the heterologous signal sequence targets the encoded protein toa vacuole, the endoplasmic reticulum, a chloroplast or a starch granule.

59. An isolated, synthetic or recombinant nucleic acid comprising asequence encoding a polypeptide having a lignocellulosic activity,wherein the sequence does not contain a signal sequence and thepolypeptide-encoding nucleic acid comprises the nucleic acid sequence ofparagraph 1 or paragraph 5.

60. A method of increasing thermotolerance or thermostability of alignocellulosic polypeptide, the method comprising glycosylating alignocellulosic enzyme, wherein the polypeptide comprises at leastthirty contiguous amino acids of the polypeptide of paragraph 19, or apolypeptide encoded by the nucleic acid of paragraph 1 or paragraph 5,thereby increasing the thermotolerance or thermostability of thelignocellulosic enzyme.

61. A method for overexpressing a recombinant lignocellulosic enzyme ina cell comprising

(A) expressing a vector comprising the nucleic acid sequence ofparagraph 1, wherein overexpression is effected by use of a highactivity promoter, a dicistronic vector or by gene amplification of thevector; or

(B) the method of (A), wherein the high activity promoter is orcomprises: a viral, bacterial, mammalian or plant promoter; or, a plantpromoter; or, a potato, rice, corn, wheat, tobacco or barley promoter;or, a constitutive promoter or a CaMV35S promoter; or, an induciblepromoter; or, a tissue-specific promoter or an environmentally regulatedor a developmentally regulated promoter; or, a seed-specific, aleaf-specific, a root-specific, a stem-specific or an abscission-inducedpromoter; or, a seed preferred promoter, a maize gamma zein promoter ora maize ADP-gpp promoter.

62. A method of making a transgenic plant comprising the followingsteps:

(A) (a) introducing a heterologous nucleic acid sequence into the cell,wherein the heterologous nucleic sequence comprises the nucleic acidsequence of paragraph 1, thereby producing a transformed plant cell; and

(b) producing a transgenic plant from the transformed cell;

(B) the method of (A), wherein the step (A)(a) further comprisesintroducing the heterologous nucleic acid sequence by electroporation ormicroinjection of plant cell protoplasts;

(C) the method of (A) or (B), comprising introducing the heterologousnucleic acid sequence directly to plant tissue by DNA particlebombardment or by using an Agrobacterium tumefaciens host; or

(D) the method of (A), (B) or (C), wherein the plant is a monocot ordicot, or the plant is a monocot corn, sugarcane, rice, wheat, barley,switchgrass or Miscanthus; or the plant is a dicot oilseed crop, soy,canola, rapeseed, flax, cotton, palm oil, sugar beet, peanut, tree,poplar or lupine.

63. A method of expressing a heterologous nucleic acid sequence in aplant cell comprising the following steps:

(A) (a) transforming the plant cell with a heterologous nucleic acidsequence operably linked to a promoter, wherein the heterologous nucleicsequence comprises the nucleic acid sequence of paragraph 1 or paragraph5; and

(b) growing the plant under conditions wherein the heterologous nucleicacids sequence is expressed in the plant cell;

(B) the method of (A), wherein the plant is a monocot or dicot, or theplant is a monocot corn, sugarcane, rice, wheat, barley, switchgrass orMiscanthus; or the plant is a dicot oilseed crop, soy, canola, rapeseed,flax, cotton, palm oil, sugar beet, peanut, tree, poplar or lupine; or

(C) the method of (A) or (B), wherein the promoter is or comprises: aviral, bacterial, mammalian or plant promoter; or, a plant promoter; or,a potato, rice, corn, wheat, tobacco or barley promoter; or, aconstitutive promoter or a CaMV35S promoter; or, an inducible promoter;or, a tissue-specific promoter or an environmentally regulated or adevelopmentally regulated promoter; or, a seed-specific, aleaf-specific, a root-specific, a stem-specific or an abscission-inducedpromoter; or, a seed preferred promoter, a maize gamma zein promoter ora maize ADP-gpp promoter.

64. A method for hydrolyzing, breaking up or disrupting acellooligsaccharide, an arabinoxylan oligomer, or a lignocellulose-,lignin-, xylan-, glucan- or cellulose-comprising composition comprisingthe following steps:

(A) (a) providing a polypeptide having a lignocellulosic activity as setforth in paragraph 19, or a polypeptide encoded by the nucleic acid ofparagraph 1 or paragraph 5, or the composition or product of manufactureof paragraphs 91 to 93 or paragraph 96;

(b) providing a composition comprising a lignocellulose, lignin, xylan,cellulose and/or glucan; and

(c) contacting the polypeptide of step (a) with the composition of step(b) under conditions wherein the lignocellulosic enzyme hydrolyzes,breaks up or disrupts the lignin-, xylan-, cellooligsaccharide,arabinoxylan oligomer, or glucan- or cellulose-comprising composition;

(B) the method of (A), wherein the composition comprises a plant cell, abacterial cell, a yeast cell, an insect cell, or an animal cell,

(C) the method of (A) or (B), wherein the polypeptide has glycosylhydrolase, endoglucanase, cellobiohydrolase, beta-glucosidase, xylanase,mannanse, β-xylosidase and/or arabinofuranosidase activity;

(D) the method of (A), (B) or (C), wherein the polypeptide of (A)(a) isa recombinant polypeptide;

(E) the method of (D), wherein the recombinant polypeptide is producedas a heterologous recombinant polypeptide within the lignocellulose-,xylan-, lignin-, glucan- or cellulose-comprising composition to behydrolyzed;

(F) the method of (D), wherein the recombinant polypeptide is producedby expression of a heterologous polynucleotide encoding the recombinantpolypeptide in a bacterium, a yeast, a plant, an insect, a fungus and ananimal, and optionally the organism is selected from the groupconsisting of an S. pombe, S. cerevisiae, Pichia pastoris, E. coli,Streptomyces sp., Bacillus sp. or a Lactobacillus sp.; or

(G) the methods of (A) to (F), wherein the lignocellulose-, lignin-,xylan-, glucan- or cellulose-comprising composition comprises: a monocotor dicot plant or plant product; or, a monocot corn, sugarcane, rice,wheat, barley, switchgrass or Miscanthus; or a dicot oilseed crop, soy,canola, rapeseed, flax, cotton, palm oil, sugar beet, peanut, tree,poplar or lupine.

65. A dough or a bread product comprising the polypeptide of paragraph19, or a polypeptide encoded by the nucleic acid of paragraph 1 orparagraph 5, or the composition or product of manufacture of paragraphs91 to 93 or paragraph 96, wherein optionally the polypeptide has aglycosyl hydrolase, cellulase, endoglucanase, cellobiohydrolase,beta-glucosidase, xylanase, mannanse, β-xylosidase and/orarabinofuranosidase activity.

66. A method of dough conditioning comprising contacting a dough or abread product with at least one polypeptide as set forth in paragraph19, or a polypeptide encoded by the nucleic acid of paragraph 1 orparagraph 5, or the composition or product of manufacture of paragraphs91 to 93 or paragraph 96, under conditions sufficient for conditioningthe dough.

67. A beverage comprising the polypeptide of paragraph 19, or apolypeptide encoded by the nucleic acid of paragraph 1 or paragraph 5,or the composition or product of manufacture of paragraphs 91 to 93 orparagraph 96, wherein optionally the polypeptide has endoglucanase,cellobiohydrolase, beta-glucosidase, xylanase, mannanse, β-xylosidaseand/or arabinofuranosidase activity.

68. A method of beverage production comprising administration of atleast one polypeptide as set forth in paragraph 19, or a polypeptideencoded by the nucleic acid of paragraph 1 or paragraph 5, or thecomposition or product of manufacture of paragraphs 91 to 93 orparagraph 96, to a beverage or a beverage precursor under conditionssufficient for decreasing the viscosity of the beverage,

wherein optionally the beverage or beverage precursor is a wort or abeer.

69. A food, a feed, food or feed supplement, or a nutritionalsupplement, comprising the polypeptide of paragraph 19, or a polypeptideencoded by the nucleic acid of paragraph 1 or paragraph 5, or thecomposition or product of manufacture of paragraphs 91 to 93 orparagraph 96, wherein optionally the polypeptide has glycosyl hydrolase,cellulase, endoglucanase, cellobiohydrolase, beta-glucosidase, xylanase,mannanse, β-xylosidase and/or arabinofuranosidase activity.

70. A method for utilizing a lignocellulosic enzyme as a nutritionalsupplement in an animal diet, the method comprising:

(A) (a) preparing a nutritional supplement containing a lignocellulosicenzyme comprising at least one polypeptide of paragraph 19, or apolypeptide encoded by the nucleic acid of paragraph 1 or paragraph 5;or the composition or product of manufacture of paragraphs 91 to 93 orparagraph 96; or

(b) administering the nutritional supplement to an animal to increaseutilization of a xylan contained in a feed or a food ingested by theanimal;

(B) the method of (A), wherein the animal is a human, or the animal is aruminant or a monogastric animal;

(C) the method of (A) or (B), wherein the lignocellulosic enzyme isprepared by expression of a polynucleotide encoding the lignocellulosicenzyme in an organism selected from the group consisting of a bacterium,a yeast, a plant, an insect, a fungus, an animal, an S. pombe, S.cerevisiae, Pichia pastoris, E. coli, Streptomyces sp., Bacillus sp. andLactobacillus sp., or a Pichia, e.g., a Pichia pastoris, aSchizosaccharomyces, e.g., a Schizosaccharomyces pombe, and/or aPseudomonas, e.g., a Pseudomonas fluorescens.

71. An edible enzyme delivery matrix or pellet comprising a thermostablerecombinant lignocellulosic enzyme comprising the polypeptide ofparagraph 19, or a polypeptide encoded by the nucleic acid of paragraph1 or paragraph 5, or the composition or product of manufacture ofparagraphs 91 to 93 or paragraph 96, wherein optionally the polypeptidehas cellulase and/or cellobiohydrolase activity.

72. A method for delivering a lignocellulosic enzyme supplement to ananimal or a human, the method comprising: preparing an edible enzymedelivery matrix or pellets comprising a granulate edible carrier and athermostable recombinant a lignocellulosic enzyme, wherein the pelletsreadily disperse the lignocellulosic enzyme contained therein intoaqueous media, and the recombinant lignocellulosic enzyme comprises thepolypeptide of paragraph 19, or a polypeptide encoded by the nucleicacid of paragraph 1 or paragraph 5, or is the composition or product ofmanufacture of paragraphs 91 to 93 or paragraph 96; and, administeringthe edible enzyme delivery matrix or pellet to the animal or human,

wherein optionally the granulate edible carrier comprises a carrierselected from the group consisting of a grain germ, a grain germ that isspent of oil, a hay, an alfalfa, a timothy, a soy hull, a sunflower seedmeal and a wheat midd,

and optionally the edible carrier comprises grain germ that is spent ofoil,

and optionally the lignocellulosic enzyme is glycosylated to providethermostability at pelletizing conditions,

and optionally the delivery matrix is formed by pelletizing a mixturecomprising a grain germ and a lignocellulosic enzyme,

and optionally the pelletizing conditions include application of steam,and optionally the pelletizing conditions comprise application of atemperature in excess of about 80° C. for about 5 minutes and the enzymeretains a specific activity of at least 350 to about 900 units permilligram of enzyme.

73. A lignocellulosic-comprising composition comprising the polypeptideof paragraph 19, or a polypeptide encoded by the nucleic acid ofparagraph 1 or paragraph 5, or the composition or product of manufactureof paragraphs 91 to 93 or paragraph 96, wherein optionally thepolypeptide has cellulase and/or cellobiohydrolase activity.

74. A wood, wood pulp, wood waste or wood product comprising alignocellulosic enzyme and/or a cellulase as set forth in paragraph 19,or a cellulase or a lignocellulosic enzyme encoded by the nucleic acidof paragraph 1 or paragraph 5, or the composition or product ofmanufacture of paragraphs 91 to 93 or paragraph 96, wherein optionallythe cellulase activity comprises cellobiohydrolase activity.

75. A paper, paper pulp or paper product comprising the polypeptide ofparagraph 19, or a polypeptide encoded by the nucleic acid of paragraph1 or paragraph 5, or the composition or product of manufacture ofparagraphs 91 to 93 or paragraph 96, wherein optionally the polypeptidehas cellulase and/or cellobiohydrolase activity.

76. A method for reducing the amount of cellulose in a paper, a wood,wood waste or wood product comprising contacting the paper, wood or woodproduct with a lignocellulosic enzyme and/or a cellulase as set forth inparagraph 19, or a lignocellulosic enzyme and/or a cellulase encoded bythe nucleic acid of paragraph 1 or paragraph 5, or the composition orproduct of manufacture of paragraphs 91 to 93 or paragraph 96, whereinoptionally the cellulase activity comprises cellobiohydrolase activity.

77. A detergent composition comprising a lignocellulosic enzyme and/or acellulase as set forth in paragraph 19, or a lignocellulosic enzyme or acellulase encoded by the nucleic acid of paragraph 1 or paragraph 5, orthe composition or product of manufacture of paragraphs 91 to 93 orparagraph 96,

wherein optionally the polypeptide is formulated in a non-aqueous liquidcomposition, a cast solid, a granular form, a particulate form, acompressed tablet, a gel form, a paste or a slurry form,

and optionally the lignocellulosic enzyme and/or cellulase activitycomprises a cellobiohydrolase activity.

78. A pharmaceutical composition or dietary supplement comprising alignocellulosic enzyme and/or a cellulase as set forth in paragraph 19,or a lignocellulosic enzyme and/or a cellulase encoded by the nucleicacid of paragraph 1 or paragraph 5, or the composition or product ofmanufacture of paragraphs 91 to 93 or paragraph 96, wherein optionallythe lignocellulosic enzyme and/or cellulase is formulated as a tablet,gel, pill, implant, liquid, spray, powder, food, feed pellet or as anencapsulated formulation

and optionally the lignocellulosic enzyme and/or cellulase activitycomprises a cellobiohydrolase activity, wherein optionally thecomposition further comprises a glucose oxidase, a glucose oxidase-1 (aβ-glucosidase) or a glucose oxidase-2 (a β-xylosidase).

79. A fuel comprising the polypeptide of paragraph 19, or a polypeptideencoded by the nucleic acid of paragraph 1 or paragraph 5, or thecomposition or product of manufacture of paragraphs 91 to 93 orparagraph 96, wherein optionally the polypeptide has activity comprisinglignocellulosic enzyme and/or a cellulase or cellobiohydrolase activity,wherein optionally the composition further comprises a glucose oxidase,a glucose oxidase-1 (a β-glucosidase) or a glucose oxidase-2 (aβ-xylosidase),

wherein optionally the fuel is derived from a plant material, whichoptionally comprises potatoes, soybean (rapeseed), barley, rye, corn,oats, wheat, beets or sugar cane,

and optionally the fuel comprises a liquid or a gas,

and optionally the fuel is a biofuel or synthetic fuel, or the fuelcomprises a bioethanol, biomethanol, biopropanol or bio-butanol, or thefuel comprises a gasoline-ethanol, methanol, propanol and/or butanolmix.

80. A method for making a fuel comprising

(A) contacting a composition comprising a cellooligsaccharide, anarabinoxylan oligomer, a lignin, a lignocellulose, a xylan, a glucan, acellulose or a fermentable sugar with the polypeptide of paragraph 19,or a polypeptide encoded by the nucleic acid of paragraph 1 or paragraph5, or the composition or product of manufacture of paragraphs 91 to 93or paragraph 96;

(B) the method of (A), wherein the composition comprising thecellooligsaccharide, arabinoxylan oligomer, lignin, lignocellulose,xylan, glucan, cellulose or fermentable sugar comprises a plant, plantproduct or plant derivative;

(C) the method of (A) or (B), wherein the plant or plant productcomprises cane sugar plants or plant products, beets or sugarbeets,wheat, corn, soybeans, potato, rice or barley;

(D) the method of (C), wherein the plant is a monocot or dicot, or theplant is a monocot corn, sugarcane, rice, wheat, barley, switchgrass orMiscanthus; or the plant is a dicot oilseed crop, soy, canola, rapeseed,flax, cotton, palm oil, sugar beet, peanut, tree, poplar or lupine;

(E) the method of (A), (B), (C) or (D), wherein the polypeptide hasactivity comprising a cellulase or cellobiohydrolase, wherein optionallythe composition further comprises a glucose oxidase, a glucose oxidase-1(a β-glucosidase) or a glucose oxidase-2 (a β-xylosidase),

(F) the method of (A), (B), (C), (D) or (E), wherein the fuel comprisesa liquid and/or a gas, or the fuel comprises a biofuel and/or asynthetic fuel, or the fuel comprises bioethanol, biomethanol,biopropanol and/or, bio-butanol; and/or a gasoline-ethanol, -methanol,-butanol and/or -propanol mix.

81. A method for making bioethanol, biomethanol, biopropanol and/or,bio-butanol comprising

(A) contacting a composition comprising a cellooligsaccharide, anarabinoxylan oligomer, a lignin, a lignocellulose, a xylan, a glucan, acellulose or a fermentable sugar with the polypeptide of paragraph 19,or a polypeptide encoded by the nucleic acid of paragraph 1 or paragraph5, or the composition or product of manufacture of paragraphs 91 to 93or paragraph 96;

(B) the method of (A), wherein the composition of comprises a plant,plant product or plant derivative, and optionally the plant or plantproduct comprises cane sugar plants or plant products, beets orsugarbeets, wheat, corn, soybeans, potato, rice or barley,

(C) the method of (A) or (B), wherein the polypeptide has activitycomprising lignocellulosic enzyme and/or a cellulase orcellobiohydrolase, wherein optionally the composition further comprisesa glucose oxidase, a glucose oxidase-1 (a β-glucosidase) or a glucoseoxidase-2 (a β-xylosidase); or

(D) the method of (A), (B) or (C), wherein the plant is a monocot ordicot, or the plant is a monocot corn, sugarcane, rice, wheat, barley,switchgrass or Miscanthus; or the plant is a dicot oilseed crop, soy,canola, rapeseed, flax, cotton, palm oil, sugar beet, peanut, tree,poplar or lupine.

(E) the method of (A), (B), (C) or (D), further comprising processingand/or formulating the bioethanol, biomethanol, biopropanol and/or,bio-butanol as a liquid fuel and/or a gas fuel, wherein optionally thefuel comprises a biofuel and/or a synthetic fuel, or the fuel comprisesbioethanol, biomethanol, biopropanol and/or, bio-butanol; and/or agasoline-ethanol, -methanol, -butanol and/or -propanol mix.

82. An enzyme ensemble, or “cocktail”, for depolymerization ofcellulosic and hemicellulosic polymers to metabolizeable carbon moietiescomprising the polypeptide of paragraph 19, or a polypeptide encoded bythe nucleic acid of paragraph 1 or paragraph 5, or the composition orproduct of manufacture of paragraphs 91 to 93 or paragraph 96, whereinoptionally the polypeptide has activity comprising lignocellulosicenzyme and/or a cellulase or cellobiohydrolase, wherein optionally thecomposition further comprises a glucose oxidase, a glucose oxidase-1 (aβ-glucosidase) or a glucose oxidase-2 (a β-xylosidase).

83. A method for processing a biomass material comprising lignocellulosecomprising contacting a composition comprising a cellulose or afermentable sugar with the polypeptide of paragraph 19, or a polypeptideencoded by the nucleic acid of paragraph 1 or paragraph 5, or thecomposition or product of manufacture of paragraphs 91 to 93 orparagraph 96,

wherein optionally the biomass material comprising lignocellulose isderived from an agricultural crop, is a byproduct of a food or a feedproduction, is a lignocellulosic waste product, or is a plant residue ora waste paper or waste paper product, and optionally the polypeptide hasactivity comprising lignocellulosic enzyme and/or cellulase orcellobiohydrolase activity, wherein optionally the composition furthercomprises a glucose oxidase, a glucose oxidase-1 (a β-glucosidase) or aglucose oxidase-2 (a β-xylosidase),

and optionally the plant residue comprise stems, leaves, hulls, husks,corn or corn cobs, corn stover, hay, straw, wood, wood chips, wood pulp,wood waste and sawdust,

and optionally the paper waste comprises discarded or used photocopypaper, computer printer paper, notebook paper, notepad paper, typewriterpaper, newspapers, magazines, cardboard and paper-based packagingmaterials,

and optionally the processing of the biomass material generates abioalcohol, a bioethanol, biomethanol, biobutanol or biopropanol.

84. A dairy product comprising the polypeptide of paragraph 19, or apolypeptide encoded by the nucleic acid of paragraph 1 or paragraph 5,or the composition or product of manufacture of paragraphs 91 to 93 orparagraph 96, wherein optionally the dairy product comprises a milk, anice cream, a cheese or a yogurt, and optionally the polypeptide hasactivity comprising a cellobiohydrolase activity.

85. A method for improving texture and flavor of a dairy productcomprising the following steps: (a) providing the polypeptide ofparagraph 19, or a polypeptide encoded by the nucleic acid of paragraph1 or paragraph 5, or the composition or product of manufacture ofparagraphs 91 to 93 or paragraph 96; (b) providing a dairy product; and(c) contacting the polypeptide of step (a) and the dairy product of step(b) under conditions wherein the lignocellulosic enzyme and/or cellulasecan improve the texture or flavor of the dairy product.

86. A textile or fabric comprising the polypeptide of paragraph 19, or apolypeptide encoded by the nucleic acid of paragraph 1 or paragraph 5,or the composition or product of manufacture of paragraphs 91 to 93 orparagraph 96, wherein optionally the textile or fabric comprises acellulose-containing fiber, and optionally the polypeptide has activitycomprising a cellobiohydrolase activity.

87. A method for treating solid or liquid animal waste productscomprising the following steps:

(a) providing the polypeptide of paragraph 19, or a polypeptide encodedby the nucleic acid of paragraph 1 or paragraph 5, or the composition orproduct of manufacture of paragraphs 91 to 93 or paragraph 96, whereinoptionally the polypeptide has activity comprising a cellobiohydrolaseactivity;

(b) providing a solid or a liquid animal waste; and

(c) contacting the polypeptide of step (a) and the solid or liquid wasteof step (b) under conditions wherein the protease can treat the waste.

88. A processed waste product comprising the polypeptide of paragraph19, or a polypeptide encoded by the nucleic acid of paragraph 1 orparagraph 5, or the composition or product of manufacture of paragraphs91 to 93 or paragraph 96, wherein optionally the polypeptide hasactivity comprising a cellobiohydrolase activity.

89. A disinfectant comprising a polypeptide having a lignocellulosicactivity, wherein the polypeptide comprises the nucleic acid sequence ofparagraph 19, or a polypeptide encoded by the nucleic acid of paragraph1 or paragraph 5, or the composition or product of manufacture ofparagraphs 91 to 93 or paragraph 96, wherein optionally the polypeptidehas activity comprising a cellobiohydrolase activity.

90. A bio-detoxifying agent or a biodefense agent comprising apolypeptide having a lignocellulosic enzyme, a cellulase and/or acellulolytic activity, wherein the polypeptide comprises the sequence ofparagraph 19, or a polypeptide encoded by the nucleic acid of paragraph1 or paragraph 5, or the composition or product of manufacture ofparagraphs 91 to 93 or paragraph 96, wherein optionally the polypeptidehas activity comprising endoglucanase, cellobiohydrolase,beta-glucosidase, xylanase, mannanse, β-xylosidase and/orarabinofuranosidase activity.

91. A composition or product of manufacture comprising

(a) a mixture (or “cocktail”) of lignocellulosic enzymes comprising: (i)at least one of each of a endoglucanase, cellobiohydrolase I (CBH I),cellobiohydrolase II (CBH II) and β-glucosidase; (ii) at least one ofeach of an xylanase, β-xylosidase and arabinofuranosidase; or, (iii) acombination of at least one of (i) or (ii); wherein the mixture of (a)comprises at least one enzyme of paragraph 19;

(b) a mixture (or “cocktail”) of hemicellulose- andcellulose-hydrolyzing enzymes comprising: (i) at least one of each of aendoglucanase, lignocellulosic enzyme, cellobiohydrolase I (CBH I),cellobiohydrolase II (CBH II), arabinofuranosidase and xylanase; (ii)the mixture of (i), wherein the glucose oxidase is a glucose oxidase-1or β-glucosidase; or (iii) the mixture of (i) or (ii), wherein theglucose oxidase is a glucose oxidase-2 or β-xylosidase; wherein themixture of (b) comprises at least one enzyme of paragraph 19;

(c) a mixture (or “cocktail”) of hemicellulose- andcellulose-hydrolyzing enzymes comprising: at least one of each of aendoglucanase; a cellobiohydrolase I (CBH I); a cellobiohydrolase II(CBH II); an arabinofuranosidase; a xylanase; a glucose oxidase-1 (aβ-glucosidase); and, a glucose oxidase-2 or β-xylosidase; wherein themixture of (c) comprises at least one enzyme of paragraph 19; or

(d) a mixture (or “cocktail”) of enzymes comprising: (1) anendoglucanase which cleaves internal β-1,4 linkages resulting in shorterglucooligosaccharides, (2) a cellobiohydrolase which acts in an “exo”manner processively releasing cellobiose units (β-1,4 glucose-glucosedisaccharide), and (3) a β-glucosidase for releasing glucose monomerfrom short cellooligosaccharides (e.g. cellobiose); wherein the mixtureof (d) comprises at least one enzyme of paragraph 19.

92. The composition or product of manufacture of paragraph 91, whereinat least one enzyme comprises an additional carbohydrate binding domain(CBM).

93. A composition or product of manufacture comprising: (a) a mixture(or “cocktail”) of enzymes as set forth in paragraph 91, or at least onelignocellulosic enzyme of paragraph 19, and a biomass material; (b) themixture of (a) wherein the biomass material comprises a lignocellulosicmaterial derived from an agricultural crop, or the biomass material is abyproduct of a food or a feed production, or the biomass material is alignocellulosic waste product, or the biomass material is a plantresidue or a waste paper or waste paper product, or the biomass materialcomprises a plant residue; (c) the mixture of (a) or (b), wherein theplant residue or the biomass material comprises sugar cane bagasse, astems, leaves, hulls, husks, corn or corn cobs, corn stover, hay, straw,wood, wood chips, wood pulp, wood waste and/or sawdust, or, the paperwaste comprises discarded or used photocopy paper, computer printerpaper, notebook paper, notepad paper, typewriter paper, newspapers,magazines, cardboard and paper-based packaging materials.

94. A method for processing a biomass material comprising

(a) providing: (i) (A) a mixture (or “cocktail”) of enzymes, or (B) thecomposition or product of manufacture of paragraphs 91 to 93 orparagraph 96; and (ii) a biomass material;

wherein the mixture (or “cocktail”) of enzymes comprises: (I) at leastone lignocellulosic enzyme of paragraph 19; or, (II) the mixture of (I),comprising a mixture (or “cocktail”) of enzymes comprisinghemicellulose- and cellulose-hydrolyzing enzymes, wherein thecellulose-hydrolyzing enzymes comprise at least one glucose oxidase,endoglucanase, cellobiohydrolase I, cellobiohydrolase II andβ-glucosidase; and the hemicellulose-hydrolyzing enzymes comprise atleast one xylanase, β-xylosidase and arabinofuranosidase,

and optionally the enzymes comprise activity comprising glucose oxidase,cellulase, endoglucanase, cellobiohydrolase, beta-glucosidase, xylanase,mannanse, β-xylosidase and/or arabinofuranosidase activity; and,

(b) contacting the mixture of enzymes with the biomass material.

95. The method of paragraph 94, wherein the biomass material comprisinglignocellulose is derived from an agricultural crop, is a byproduct of afood or a feed production, is a lignocellulosic waste product, or is aplant residue or plant material, or a waste paper or waste paperproduct, and optionally the plant residue or plant material comprisesugar cane bagasse, stems, leaves, hulls, husks, corn or corn cobs, cornstover, hay or straw, wood, wood chips, wood pulp, wood waste andsawdust, and optionally the paper waste comprises discarded or usedphotocopy paper, computer printer paper, notebook paper, notepad paper,typewriter paper, newspapers, magazines, cardboard and paper-basedpackaging materials, and optionally the processing of the biomassmaterial generates a bioethanol.

96. A mixture or cocktail of enzymes comprising

(a) at least one lignocellulosic enzyme of paragraph 19;

(b) a combination of enzymes as set forth in paragraph 19;

(c) at least one of each of a endoglucanase, cellobiohydrolase I (CBHI), cellobiohydrolase II (CBH II) and β-glucosidase; (ii) at least oneof each of an xylanase, β-xylosidase and arabinofuranosidase; or, (iii)a combination of at least one of (i) or (ii); wherein the mixturecomprises at least one enzyme of paragraph 19;

(d) at least one hemicellulose- and/or cellulose-hydrolyzing enzymecomprising: (i) at least one of each of a endoglucanase, glucoseoxidase, cellobiohydrolase I (CBH I), cellobiohydrolase II (CBH II),arabinofuranosidase and xylanase; (ii) the mixture of (i), wherein theglucose oxidase is a glucose oxidase-1 or β-glucosidase; and/or (iii)the mixture of (i) or (ii), wherein the glucose oxidase is a glucoseoxidase-2 or β-xylosidase; wherein the mixture comprises at least oneenzyme of paragraph 19;

(e) at least one hemicellulose- and/or cellulose-hydrolyzing enzymecomprising: at least one of each of a endoglucanase; a cellobiohydrolaseI (CBH I); a cellobiohydrolase II (CBH II); an arabinofuranosidase; axylanase; a glucose oxidase-1 (a β-glucosidase); and/or, a glucoseoxidase-2 or β-xylosidase; wherein the mixture of (c) comprises at leastone enzyme of paragraph 19; or

(f) at least one (1) endoglucanase which cleaves internal β-1,4 linkagesresulting in shorter glucooligosaccharides, (2) cellobiohydrolase whichacts in an “exo” manner processively releasing cellobiose units (β-1,4glucose-glucose disaccharide), and/or (3) β-glucosidase for releasingglucose monomer from short cellooligosaccharides (e.g. cellobiose);wherein the mixture of (d) comprises at least one enzyme of paragraph19.

97. A method for processing a biomass material comprising

(a) (i) providing a mixture of enzymes as set forth in paragraph 96; and

(ii) contacting the enzyme mixture with the biomass material;

(b) the process of (a), wherein the biomass material comprisinglignocellulose is derived from an agricultural crop, is a byproduct of afood or a feed production, is a lignocellulosic waste product, or is aplant material, plant byproduct of a process, or a plant residue, or awaste paper or waste paper product;

(c) the process of (a) or (b), wherein the polypeptide has activitycomprising glucose oxidase, cellulase, endoglucanase, cellobiohydrolase,beta-glucosidase, xylanase, mannanse, β-xylosidase and/orarabinofuranosidase activity;

(d) the process of (a), (b) or (c), wherein the wherein the biomassmaterial comprises a plant residue comprising sugar cane bagasse, stems,leaves, hulls, husks, corn or corn cobs, corn stover, hay or straw,wood, wood chips, wood pulp, a paper waste, wood waste and/or sawdust;

(e) the process of (d), wherein the paper waste comprises discarded orused photocopy paper, computer printer paper, notebook paper, notepadpaper, typewriter paper, newspapers, magazines, cardboard andpaper-based packaging materials;

(f) the process of (a), (b), (c), (d) or (e), further comprisingprocessing the biomass material to generate a carbohydrate, bioethanoland/or an alcohol.

98. A chimeric polypeptide comprising

(a) a first domain and at least a second domain, wherein the firstdomain comprises an enzyme of paragraph 19, and the second domaincomprises a heterologous or modified carbohydrate binding domain (CBM),a heterologous or modified dockerin domain, a heterologous or modifiedprepro domain, or a heterologous or modified active site;

(b) the chimeric polypeptide of (a), wherein the carbohydrate bindingdomain (CBM) is a cellulose-binding module or a lignin-binding domain;

(c) the chimeric polypeptide of (a) or (b), wherein the CBM isapproximate to the enzyme's catalytic domain;

(d) the chimeric polypeptide of (a), (b) or (c), wherein the at leastone CBM is positioned approximate to the polypeptide's catalytic domain;

(e) the chimeric polypeptide of (d), wherein the at least one CBM ispositioned: approximate to the C-terminus of the polypeptide's catalyticdomain, or, approximate to the N-terminus of the polypeptide's catalyticdomain, or both;

(f) the chimeric polypeptide of any of (a), (b), (c) or (e), wherein thechimeric polypeptide is a recombinant chimeric protein.

99. A chimeric polypeptide comprising

(a) a polypeptide of paragraph 19 having a lignocellulosic enzymeactivity, and a domain comprising at least one heterologous or modifiedcarbohydrate binding domain (CBM), or at least one internally rearrangedCBM, or any combination thereof.

What is claimed is:
 1. A polypeptide comprising the amino acid sequenceof a variant cellobiohydrolase I (“CBH I”) catalytic domain, saidvariant CBH I catalytic domain having at least 90% sequence identity toa reference catalytic domain corresponding to amino acid positions26-455 of SEQ ID NO:134, and which comprises a N222H amino acidsubstitution that results in increased activity as compared to thereference catalytic domain.
 2. The polypeptide of claim 1, furthercomprising one or more of the following substitutions or combinations ofsubstitutions: (a) N222E; (b) S217K; (c) L225Y; (d) L225V; (e) D87L; (f)G256I; (g) H157G; (h) P159G; (i) N183A; (j) S156G; (k) S218P+T316S; (l)D318Q+T322S+1363V; (m) T324R; (n) S326L; (o) Q334S; (p) K345D; (q)K45R+T293A+S350C; (r) G351D; (s) N352V; (t) F358L; (u) A3701; (v) G376R;(w) E386S; (x) V451W; (y) N455G; (z)Y31L+T32Q+S72A+T73Q+T77D+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (aa)Y31L+S72W+T77D+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (bb)S72Y+T73Q+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (cc)Y31L+T32W+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (dd)T32Q+F120-VTGSNVG-S128→F120-VTKGSFSSNIG-S132; (ee)Y31Q+T32Q+S72Y+T77D+F120-VTGSNVG-S128→F120-VTQSAQKNVG-A131; (ff)Y31A+T32Y+S72Y+T73Y+T77D; (gg) Y31Q+T32Q+S72Y+T73Y+T77D; (hh)T32W+T73W+T77D; (ii) Y31A+T32Q+T73Y+T77D; (jj)S72W+T73Q+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (kk)Y31L+T32Y+T77D+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (ll)P159G+S217K+N222H+L225Y+K345D+N352V+V451W; (mm)L225Y+K345D+N352V+E386S+V451W; (nn) S326L+K345D+N352V; (oo)L225Y+D318Q+T324R+S326L+K345D+E386S; (pp)P159G+S217K+L225Y+Q334S+K345D+E386S; and (qq) E386S+V451W.
 3. Thepolypeptide of claim 1, wherein the variant CBH I catalytic domaincomprises an amino acid sequence having at least 95% sequence identityto amino acid positions 26-455 of SEQ ID NO:134.
 4. The polypeptide ofclaim 1 in which the variant CBH I catalytic domain is operably linkedto a heterologous cellulose binding domain.
 5. The polypeptide of claim4 in which catalytic domain is operably linked to a cellulose bindingdomain via a linker.
 6. The polypeptide of claim 5 in which thecellulose binding domain is C-terminal to the catalytic domain.
 7. Thepolypeptide of claim 5 in which the cellulose binding domain isN-terminal to the catalytic domain.
 8. The polypeptide of claim 7 whichis a mature polypeptide.
 9. The polypeptide of claim 7 which furthercomprises a signal sequence.
 10. A composition comprising a polypeptideaccording to claim
 1. 11. The composition of claim 10 in which saidpolypeptide represents at least 5% of all polypeptides in saidcomposition.
 12. The composition of claim 11 in which said polypeptiderepresents at least 25% of all polypeptide in said composition.
 13. Thecomposition of claim 10 which is a whole cellulase.
 14. The compositionof claim 13, wherein the whole cellulase is produced by a host cell thatrecombinantly expresses said polypeptide.
 15. The composition of claim14 which is filamentous fungal whole cellulase.
 16. A fermentation brothcomprising a polypeptide according to claim
 1. 17. The fermentationbroth of claim 16, which is a filamentous fungal fermentation broth. 18.The fermentation broth of claim 17 which is a cell-free fermentationbroth.
 19. A polypeptide comprising a variant CBH I amino acid sequence,said variant CBH I amino acid sequence having at least 90% sequenceidentity to a reference CBH I corresponding to amino acid positions26-529 of SEQ ID NO:134, and which comprises a N222H amino acidsubstitutions that result in increased activity as compared to thereference to the reference CBH I.
 20. The polypeptide of claim 19, whichhas one or more of the following substitutions or combinations ofsubstitutions: (a) N222E; (b) S217K; (c) L225Y; (d) L225V; (e) H497S;(f) T510K; (g) D87L; (h) G256I; (i) H157G; (j) P159G; (k) N183A; (l)S156G; (m) S218P+T316S; (n) D318Q+T322S+1363V; (o) T324R; (p) S326L; (q)□334S; (r) K345D; (s) K45R+T293A+S350C; (t) G351D; (u) N352V; (v) F358L;(w) A3701; (x) G376R; (y) E386S; (z) V451W; (aa) N455G; (bb) S463K; (cc)Y31L+T32Q+S72A+T73Q+T77D+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (dd)Y31L+S72W+T77D+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (ee)S72Y+T73Q+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (ff)Y31L+T32W+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (gg)T32Q+F120-VTGSNVG-S128→F120-VTKGSFSSNIG-S132; (hh)Y31Q+T32Q+S72Y+T77D+F120-VTGSNVG-S128→F120-VTQSAQKNVG-A131; (ii)Y31A+T32Y+S72Y+T73Y+T77D; (jj) Y31Q+T32Q+S72Y+T73Y+T77D; (kk)T32W+T73W+T77D; (ll) Y31A+T32Q+T73Y+T77D; (mm)S72W+T73Q+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (nn)Y31L+T32Y+T77D+F120-VTGSNVG-5128→F120-VQQGPYSKNVG-S132; (oo)P159G+S217K+N222H+L225Y+K345D+N352V+V451W; (pp)N222H+L225Y+K345D+N352V+E386S+V451W; (qq) S326L+K345D+N352V; (rr)L225Y+D318Q+T324R+S326L+K345D+E386S; (ss)P159G+S217K+N222H+L225Y+Q334S+K345D+E386S; and (tt) E386S+V451W.
 21. Thepolypeptide of claim 19, wherein the variant CBH I catalytic domaincomprises an amino acid sequence having at least 95% sequence identityto amino acid positions 26-529 of SEQ ID NO:134.
 22. The polypeptide ofclaim 19 which is a mature polypeptide.
 23. The polypeptide claim 19which further comprises a signal sequence.
 24. A nucleic acid comprisinga nucleotide sequence encoding the polypeptide claim
 1. 25. A vectorcomprising the nucleic acid of claim
 24. 26. The vector of claim 25which further comprises an origin of replication.
 27. The vector ofclaim 25 which further comprises a promoter sequence operably linked tosaid nucleotide sequence.
 28. The vector of claim 27, wherein thepromoter sequence is operable in yeast.
 29. The vector of claim 27,wherein the promoter sequence is operable in filamentous fungi.
 30. Arecombinant cell engineered to express the nucleic acid of claim
 24. 31.The recombinant cell of claim 30 which is a eukaryotic cell.
 32. Therecombinant cell of claim 31 which is a filamentous fungal cell.
 33. Therecombinant cell of claim 32, wherein the filamentous fungal cell is ofthe genus Aspergillus, Penicillium, Rhizopus, Chrysosporium,Myceliophthora,Trichoderma, Humicola, Acremonium or Fusarium.
 34. Therecombinant cell of claim 32, wherein the filamentous fungal cell is ofthe species Aspergillus niger, Aspergillus oryzae, Trichoderma reesei,Penicillium chrysogenum, Myceliophthora thermophila, or Rhizopus oryzae.35. The recombinant cell of claim 31 which is a yeast cell.
 36. Therecombinant cell of claim 35 which is a yeast cell of the genusSaccharomyces, Kluyveromyces, Candida, Pichia, Schizosaccharomyces,Hansenula, Klockera, Schwanniomyces or Yarrowia.
 37. The recombinantcell of claim 36, wherein the yeast cell is of the species S.cerevisiae, S. bulderi, S. barnetti, S. exiguus, S. uvarum, S.diastaticus, K. lactis, K. marxianus or K. fragilis.
 38. The recombinantcell of claim 37, which is a S. cerevisiae cell.
 39. A host celltransformed with the vector of claim
 25. 40. The host cell of claim 39which is a prokaryotic cell.
 41. The host cell of claim 40 which is abacterial cell.
 42. The host cell of claim 39 which is a eukaryoticcell.
 43. A method of producing a polypeptide according to claim 1comprising culturing the recombinant cell engineered to express saidpolypeptide under conditions in which the polypeptide is expressed. 44.The method of claim 43, wherein the polypeptide comprises a signalsequence and wherein the recombinant cell is cultured under conditionsin which the polypeptide is secreted from the recombinant cell.
 45. Themethod of claim 44, further comprising recovering the polypeptide fromthe cell culture.
 46. The method of claim 45, wherein recovering thepolypeptide comprises a step of centrifuging away cells and/or cellulardebris.
 47. The method of claim 45, wherein recovering the polypeptidecomprises a step of filtering away cells and/or cellular debris.
 48. Apolypeptide comprising the amino acid sequence of a variantcellobiohydrolase I (“CBH I”) catalytic domain, said variant CBH Icatalytic domain having at least 90% sequence identity to a referencecatalytic domain corresponding to amino acid positions 26-455 of SEQ IDNO: 134, and which comprises a V121T amino acid substitution thatresults in increased activity as compared to the reference catalyticdomain.
 49. The polypeptide of claim 48, further comprising one or moreof the following substitutions or combinations of substitutions: (a)V121S; (b)Y31L+T32Q+S72A+T73Q+T77D+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (c)Y31L+S72W+T77D+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (d)S72Y+T73Q+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (e)Y31L+T32W+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (g)T32Q+F120-VTGSNVG-S128→F120-VTKGSFSSNIG-S132; (f)Y31Q+T32Q+S72Y+T77D+F120-VTGSNVG-S128→F120-VTQSAQKNVG-A131; (f)Y31A+T32Y+S72Y+T73Y+T77D; (h) Y31Q+T32Q+S72Y+T73Y+T77D; (i)T32W+T73W+T77D; (j) Y31A+T32Q+T73Y+T77D; (k)S72W+T73Q+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; and (l)Y31L+T32Y+T77D+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132.
 50. Acomposition comprising the polypeptide of claim
 48. 51. A nucleic acidcomprising a nucleotide sequence encoding the polypeptide of claim 48.52. A vector comprising the nucleic acid of claim
 51. 53. The vector ofclaim 52 which further comprises an origin of replication.
 54. Thevector of claim 53 which further comprises a promoter sequence operablylinked to said nucleotide sequence.
 55. The vector of claim 54, whereinthe promoter sequence is operable in yeast.
 56. The vector of claim 54,wherein the promoter sequence is operable in filamentous fungi.
 57. Arecombinant cell engineered to express the nucleic acid of claim
 51. 58.The recombinant cell of claim 57 which is a eukaryotic cell.
 59. Therecombinant cell of claim 58 which is a yeast cell.
 60. The recombinantcell of claim 59 which is a yeast cell of the genus Saccharomyces,Kluyveromyces, Candida, Pichia, Schizosaccharomyces, Hansenula,Klockera, Schwanniomyces or Yarrowia.
 61. The recombinant cell of claim59, wherein the yeast cell is of the species S. cerevisiae, S. bulderi,S. barnetti, S. exiauus, S. uvarum, S. diastaticus, K. lactis, K.marxilanus or K. fragilis.
 62. The recombinant cell of claim 61, whichis a S. cerevisiae cell.
 63. The recombinant cell of claim 58 which is afilamentous fungal cell.
 64. The recombinant cell of claim 63, whereinthe filamentous fungal cell is of the genus Aspergillus, Penicillium,Rhizopus, Chrysosporium, Myceliophthora, Trichoderma, Humicola,Acremonium or Fusarium.
 65. The recombinant cell of claim 63, whereinthe filamentous fungal cell is of the species Aspergillus niger,Aspergillus oryzae, Trichoderma reesei, Penicillium chrysogenum,Myceliophthora thermophila, or Rhizopus oryzae.
 66. A host celltransformed with the vector of claim
 52. 67. The host cell of claim 66which is a prokaryotic cell.
 68. The host cell of claim 67 which is abacterial cell.
 69. The host cell of claim 66 which is a eukaryoticcell.
 70. A method of producing a polypeptide according to claim 48comprising culturing the recombinant cell engineered to express saidpolypeptide under conditions in which the polypeptide is expressed. 71.The method of claim 70, wherein the polypeptide comprises a signalsequence and wherein the recombinant cell is cultured under conditionsin which the polypeptide is secreted from the recombinant cell.
 72. Themethod of claim 71, further comprising recovering the polypeptide fromthe cell culture.
 73. The method of claim 72, wherein recovering thepolypeptide comprises a step of centrifuging away cells and/or cellulardebris.
 74. The method of claim 72, wherein recovering the polypeptidecomprises a step of filtering away cells and/or cellular debris.
 75. Apolypeptide comprising the amino acid sequence of a variantcellobiohydrolase I (“CBH I”) catalytic domain, said variant CBH Icatalytic domain having at least 90% sequence identity to a referencecatalytic domain corresponding to amino acid positions 26-455 of SEQ IDNO: 134, and which comprises a V392A +V401A+T417A amino acidsubstitution that results in improved thermotolerance as compared to thereference catalytic domain.
 76. The polypeptide of claim 75, furthercomprising one or more of the following substitutions or combinations ofsubstitutions: (a) S104N; (b) V121S; (c) V121T; (d) G113N; (e) L116T;(f) T268V; (g) T35A+V401A; (h) V392T; (i) Y399D; (j) V401D; (k) L404T;(I) S463Y; (m) A221V+V401A+G474W; and (n) A472M.
 77. A compositioncomprising the polypeptide of claim
 75. 78. A nucleic acid comprising anucleotide sequence encoding the polypeptide of claim
 75. 79. A vectorcomprising the nucleic acid of claim
 78. 80. The vector of claim 79which further comprises an origin of replication.
 81. The vector ofclaim 80 which further comprises a promoter sequence operably linked tosaid nucleotide sequence.
 82. The vector of claim 81, wherein thepromoter sequence is operable in yeast.
 83. The vector of claim 81,wherein the promoter sequence is operable in filamentous fungi.
 84. Arecombinant cell engineered to express the nucleic acid of claim
 78. 85.The recombinant cell of claim 84 which is a eukaryotic cell.
 86. Therecombinant cell of claim 85 which is a filamentous fungal cell.
 87. Therecombinant cell of claim 86, wherein the filamentous fungal cell is ofthe genus Aspergilius, Penicillium, Rhizopus, Chrysosporium,Myceliophthora, Trichoderma, Humicola, Acremonium or Fusarium.
 88. Therecombinant cell of claim 86, wherein the filamentous fungal cell is ofthe species Aspergillus niger, Aspergillus oryzae, Trichoderma reesei,Penicillium chrysogenum, Myceliophthora thermophila, or Rhizopus oryzae.89. The recombinant cell of claim 85 which is a yeast cell.
 90. Therecombinant cell of claim 89 which is a yeast cell of the genusSaccharomyces, Kluyveromyces, Candida, Pichia, Schizosaccharomyces,Hansenula, Klockera, Schwanniomyces or Yarrowia.
 91. The recombinantcell of claim 89, wherein the yeast cell is of the species S.cerevisiae, S. bulderi, S. barnetti, S. exiguus, S. uvarum, S.diastaticus, K. lactis, K. marxianus or K. fragilis.
 92. The recombinantcell of claim 91, which is a S. cerevisiae cell.
 93. A host celltransformed with the vector of claim
 79. 94. The host cell of claim 93which is a prokaryotic cell.
 95. The host cell of claim 94 which is abacterial cell.
 96. The host cell of claim 93 which is a eukaryoticcell.
 97. A method of producing a polypeptide according to claim 75comprising culturing the recombinant cell engineered to express saidpolypeptide under conditions in which the polypeptide is expressed. 98.The method of claim 97, wherein the polypeptide comprises a signalsequence and wherein the recombinant cell is cultured under conditionsin which the polypeptic is secreted from the recombinant cell.
 99. Themethod of claim
 98. further comprising recovering the polypeptide fromthe cell culture.
 100. The method of claim 99, wherein recovering thepolypeptide comprises a step of centrifuging away cells and/or cellulardebris.
 101. The method of claim 99, wherein recovering the polypeptidecomprises a step of filtering away cells and/or cellular debris.
 102. Apolypeptide comprising the amino acid sequence of a variantcellobiohydrolase I (“CBH I”) catalytic domain, said variant CBH Icatalytic domain having at least 90% sequence identity to a referencecatalytic domain corresponding to amino acid positions 26-455 of SEQ IDNO: 134, and which comprises a V121T amino acid substitution thatresults in increased thermotolerance as compared to the referencecatalytic domain.
 103. The polypeptide of claim 102, further comprisingone or more of the following substitutions or combinations ofsubstitutions: (a) V121S; (b)Y31L+T32Q+S72A+T73Q+T77D+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (c)Y31L+S72W+T77D+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (d)S72Y+T73Q+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (e)Y31L+T32W+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; (g)T32Q+F120-VTGSNVG-S128→F120-VTKGSFSSNIG-S132; (f)Y31Q+T32Q+S72Y+T77D+F120-VTGSNVG-S128→F120-VTQSAQKNVG-A131; (f)Y31A+T32Y+S72Y+T73Y+T77D; (h) Y31Q+T32Q+S72Y+T73Y+T77D; (i)T32W+T73W+T77D; (j) Y31A+T32Q+T73Y+T77D; (k)S72W+T73Q+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132; and (l)Y31L+T32Y+T77D+F120-VTGSNVG-S128→F120-VQQGPYSKNVG-S132.
 104. Acomposition comprising the polypeptide of claim
 102. 105. A nucleic acidcomprising a nucleotide sequence encoding the polypeptide of claim 102.106. A vector comprising the nucleic acid of claim
 105. 107. The vectorof claim 106 which further comprises an origin of replication.
 108. Thevector of claim 107 which further comprises a promoter sequence operablylinked to said nucleotide sequence.
 109. The vector of claim 108,wherein the promoter sequence is operable in yeast.
 110. The vector ofclaim 108, wherein the promoter sequence is operable in filamentousfungi.
 111. A recombinant cell engineered to express the nucleic acid ofclaim
 105. 112. The recombinant cell of claim 111 which is a eukaryoticcell.
 113. The recombinant cell of claim 112 which is a filamentousfungal cell.
 114. The recombinant cell of claim 113, wherein thefilamentous fungal cell is of the genus Aspergillus, Penicillium,Rhizopus, Chrysosporium, Mycellophthora, Trichoderma, Humicola,Acremonium or Fusarium.
 115. The recombinant cell of claim 113, whereinthe filamentous fungal cell is of the species Aspergillus niger,Aspergillus oryzae, Trichoderma reesei, Penicillium chrysogenum,Myceliophthora thermophila, or Rhizopus oryzae.
 116. The recombinantcell of claim 112 which is a yeast cell.
 117. The recombinant cell ofclaim 116 which is a yeast cell of the genus Saccharomyces,Kluyveromyces, Candida, Pichia, Schizosaccharomyces, Hansenula,Klockera, Schwanniomyces or Yarrowia.
 118. The recombinant cell of claim116, wherein the yeast cell is of the species S. cerevisiae, S. bulderi,S. barnetti, S. exiguus, S. uvarum, S. diastaticus, K. lactis, K.marxianus or K. fragilis.
 119. The recombinant cell of claim 118, whichis a S. cerevisiae cell.
 120. A host cell transformed with the vector ofclaim
 106. 121. The host cell of claim 120 which is a prokaryotic cell.122. The host cell of claim 121 which is a bacterial cell.
 123. The hostcell of claim 120 which is a eukaryotic cell.
 124. A method of producinga polypeptide according to claim 102 comprising culturing therecombinant cell engineered to express said polypeptide under conditionsin which the polypeptide is expressed.
 125. The method of claim 124,wherein the polypeptide comprises a signal sequence and wherein therecombinant cell is cultured under conditions in which the polypeptideis secreted from the recombinant cell.
 126. The method of claim 125,further comprising recovering the polypeptide from the cell culture.127. The method of claim 126, wherein recovering the polypeptidecomprises a step of centrifuging away cells and/or cellular debris. 128.The method of claim 126, wherein recovering the polypeptide comprises astep of filtering away cells and/or cellular debris.
 129. A polypeptidecomprising a variant cellobiohydrolase I (“CBH I”) catalytic domainamino acid sequence, said variant CBH I amino acid sequence having atleast 90% sequence identity to a reference CBH I corresponding to aminoacid positions 26-529 of SEQ ID NO:134, and which comprises a V121Samino acid substitution that result in-improved thermotolerance ascompared to the reference to the reference CBH I.
 130. The polypeptideof claim 129, further comprising one or more of the followingsubstitutions or combinations of substitutions: (a) S104N; (b) V121T;(c) G113N; (d) L116T; (e) T268V; (f) T35A+V401A; (g) V392T; (h) Y399D;(i) V401D; (j) V392A+V401A+T417A; (k) L404T; (l) S463Y; (m)A221V+V401A+G474W; (n) A472M; and (o) V401A+V494L.
 131. A compositioncomprising the polypeptide of claim
 129. 132. A nucleic acid comprisinga nucleotide sequence encoding the polypeptide of claim
 129. 133. Avector comprising the nucleic acid of claim
 132. 134. The vector ofclaim 133 which further comprises an origin of replication.
 135. Thevector of claim 134 which further comprises a promoter sequence operablylinked to said nucleotide sequence.
 136. The vector of claim 135,wherein the promoter sequence is operable in yeast.
 137. The vector ofclaim 135, wherein the promoter sequence is operable in filamentousfungi.
 138. A recombinant cell engineered to express the nucleic acid ofclaim
 132. 139. The recombinant cell of claim 138 which is a eukaryoticcell.
 140. The recombinant cell of claim 139 which is a filamentousfungal cell.
 141. The recombinant cell of claim 140, wherein thefilamentous fungal cell is of the genus Aspergilius, Penicillium,Rhizopus, Chrysosporium, Myceliophthora, Trichoderma, Humicola,Acremonium or Fusarium.
 142. The recombinant cell of claim 140, whereinthe filamentous fungal cell is of the species Aspergillus niger,Aspergillus oryzae, Trichoderma reesei, Penicillium chrysogenum,Myceliophthora therrnophila, or Rhizopus oryzae.
 143. The recombinantcell of claim 139 which is a yeast cell.
 144. The recombinant cell ofclaim 143 which is a yeast cell of the genus Saccharomyces,Kluyveromyces, Candida, Pichia, Schizosaccharomyces, Hansenula,Klockera, Schwanniomyces or Yarrowia.
 145. The recombinant cell of claim143, wherein the yeast cell is of the species S. cerevisiae, S. bulderi,S. barnetti, S. exiguus, S. uvarum, S. diastaticus, K. lactis, K.marxianus or K. fragilis.
 146. The recombinant cell of claim 145, whichis a S. cerevisiae cell.
 147. A host cell transformed with the vector ofclaim
 133. 148. The host cell of claim 147 which is a prokaryotic cell.149. The host cell of claim 148 which is a bacterial cell.
 150. The hostcell of claim 147 which is a eukaryotic cell.
 151. A method of producinga polypeptide according to claim 129 comprising culturing therecombinant cell engineered to express said polypeptide under conditionsin which the polypeptide is expressed.
 152. The method of claim 151,wherein the polypeptide comprises a signal sequence and wherein therecombinant cell is cultured under conditions in which the polypeptic issecreted from the recombinant cell.
 153. The method of claim 152,further comprising recovering the polypeptide from the cell culture.154. The method of claim 153, wherein recovering the polypeptidecomprises a step of centrifuging away cells and/or cellular debris. 155.The method of claim 153, wherein recovering the polypeptide comprises astep of filtering away cells and/or debris.
 156. A method forsaccharifying biomass, comprising: treating biomass with a compositionaccording to claim
 10. 157. The method of claim 156, further comprisingrecovering monosaccharides.
 158. A method for producing ethanol,comprising: (a) treating biomass with a composition according to claim10, thereby producing monosaccharides; and (b) culturing a fermentingmicroorganism in the presence of the monosaccharides produced in step(a) under fermentation conditions, thereby producing ethanol.
 159. Themethod of claim 158, further comprising, prior to step (a), pretreatingthe biomass.
 160. The method of claim 158, wherein said fermentingmicroorganism is a bacterium or a yeast.
 161. The method of claim 160,wherein said fermenting microorganism is a bacterium selected fromZymomonas mobilis, Escherichia coli and Klebsiella oxytoca.
 162. Themethod of claim 160, wherein said fermenting microorganism is a yeastselected from Saccharomyces cerevisiae, Saccharomyces uvarum,Kluyveromyces fragilis, Kluyveromyces lactis, Candida pseudotropicalis,and Pachysolen tannophilus.
 163. The method of claim 158, wherein saidbiomass is corn stover, bagasses, sorghum, giant reed, elephant grass,miscanthus, Japanese cedar, wheat straw, switchgrass, hardwood pulp,softwood pulp, crushed sugar cane, energy cane, or Napier grass.
 164. Amethod for saccharifying biomass, comprising: treating biomass with acomposition with a fermentation broth according to claim
 17. 165. Amethod for producing ethanol, comprising: (a) treating biomass with afermentation broth according to claim 17, thereby producingmonosaccharides; and (b) culturing a fermenting microorganism in thepresence of the monosaccharides produced in step (a) under fermentationconditions, thereby producing ethanol.
 166. A method for saccharifyingbiomass, comprising: treating biomass with a composition according toclaim
 50. 167. The method of claim 166, further comprising recoveringmonosaccharides.
 168. A method for producing ethanol, comprising: (a)treating biomass with a composition according to claim 50, therebyproducing monosaccharides; and (b) culturing a fermenting microorganismin the presence of the monosaccharides produced in step (a) underfermentation conditions, thereby producing ethanol.
 169. The method ofclaim 168, further comprising, prior to step (a), pretreating thebiomass.
 170. The method of claim 168, wherein said fermentingmicroorganism is a bacterium or a yeast.
 171. The method of claim 170,wherein said fermenting microorganism is a bacterium selected fromZymomonas mobilis, Escherichia coli and Klebsiella oxytoca.
 172. Themethod of claim 170, wherein said fermenting microorganism is a yeastselected from Saccharomyces cerevisiae, Saccharomyces uvarum,Kluyveromyces fragilis, Kluyyeromyces lactis, Candida pseudotropicalis,and Pachysolen tannophilus.
 173. The method of claim 168, wherein saidbiomass is corn stover, bagasses, sorghum, giant reed, elephant grass,miscanthus, Japanese cedar, wheat straw, switchgrass, hardwood pulp,softwood pulp, crushed sugar cane, energy cane, or Napier grass.
 174. Amethod for saccharifying biomass, comprising: treating biomass with acomposition according to claim
 77. 175. The method of claim 174, furthercomprising recovering monosaccharides.
 176. A method for producingethanol, comprising; (a) treating biomass with a composition accordingto claim 77, thereby producing monosaccharides; and (b) culturing afermenting microorganism in the presence of the monosaccharides producedin step (a) under fermentation conditions, thereby producing ethanol.177. The method of claim 176, further comprising, prior to step (a),pretreating the biomass.
 178. The method of claim 176, wherein saidfermenting microorganism is a bacterium or a yeast.
 179. The method ofclaim 178, wherein said fermenting microorganism is a bacterium selectedfrom Zymomonas mobilis, Escherichia coli and Klebsiella oxytoca. 180.The method of claim 178, wherein said fermenting microorganism is ayeast selected from Saccharomyces cerevisiae, Saccharomyces uvarum,Kluyveromyces fragilis, Kluyveromyces lactis, Candida pseudotropicalis,and Pachysolen tannophilus.
 181. The method of claim 176, wherein saidbiomass is corn stover, bagasses, sorghum, giant reed, elephant grass,miscanthus, Japanese cedar, wheat straw, switchgrass, hardwood pulp,softwood pulp, crushed sugar cane, energy cane, or Napier grass.
 182. Amethod for saccharifying biomass, comprising: treating biomass with acomposition according to claim
 104. 183. The method of claim 182,further comprising recovering monosaccharides.
 184. A method forproducing ethanol, comprising: (a) treating biomass with a compositionaccording to claim 104, thereby producing monosaccharides; and (b)culturing a fermenting microorganism in the presence of themonosaccharides produced in step (a) under fermentation conditions,thereby producing ethanol.
 185. The method of claim 184, furthercomprising, prior to step (a), pretreating the biomass.
 186. The methodof claim 184, wherein said fermenting microorganism is a bacterium or ayeast.
 187. The method of claim 186, wherein said fermentingmicroorganism is a bacterium selected from Zymomonas mobilis,Escherichia coli and Klebsiella oxytoca.
 188. The method of claim 186,wherein said fermenting microorganism is a yeast selected fromSaccharornyces cerevisiae, Saccharomyces uvarum, Kluyveromyces fragilis,Kluyveromyces lactis, Candida pseudotropicalis, and Pachysolentannophilus.
 189. The method of claim 184, wherein said biomass is cornstover, bagasses, sorghum, giant reed, elephant grass, miscanthus,Japanese cedar, wheat straw, switchgrass, hardwood pulp, softwood pulp,crushed sugar cane, energy cane, or Napier grass.
 190. A method forsaccharifying biomass, comprising: treating biomass with a compositionaccording to claim
 131. 191. The method of claim 190, further comprisingrecovering monosaccharides.
 192. A method for producing ethanol,comprising: (a) treating biomass with a composition according to claim131, thereby producing monosaccharides; and (b) culturing a fermentingmicroorganism in the presence of the monosaccharides produced in step(a) under fermentation conditions, thereby producing ethanol.
 193. Themethod of claim 192, further comprising, prior to step (a), pretreatingthe biomass.
 194. The method of claim 192, wherein said fermentingmicroorganism is a bacterium or a yeast.
 195. The method of claim 194,wherein said fermenting microorganism is a bacterium selected fromZymomonas mobilis, Escherichia coli and Klebsiella oxytoca.
 196. Themethod of claim 194, wherein said fermenting microorganism is a yeastselected from Saccharomyces cerevisiae, Saccharomyces uvarum,Kluyverornyces fragilis, Kluyveromyces lactis, Candida pseudotropicalis,and Pachysoien tannophilus.
 197. The method of claim 192, wherein saidbiomass is corn stover, bagasses, sorghum, giant reed, elephant grass,miscanthus, Japanese cedar, wheat straw, switchorass, hardwood pulp,softwood pulp, crushed sugar cane, energy cane, or Napier grass.